{"id":1167,"date":"2024-05-26T11:30:03","date_gmt":"2024-05-26T08:30:03","guid":{"rendered":"https:\/\/www.bioeng.ru\/structbiotech\/?page_id=1167"},"modified":"2024-11-07T20:05:24","modified_gmt":"2024-11-07T17:05:24","slug":"shaperonins","status":"publish","type":"page","link":"https:\/\/www.bioeng.ru\/structbiotech\/en\/shaperonins\/","title":{"rendered":"Chaperonins"},"content":{"rendered":"<div data-elementor-type=\"wp-page\" data-elementor-id=\"1167\" class=\"elementor elementor-1167\">\n\t\t\t\t<div class=\"elementor-element elementor-element-5a2cce4e e-con-full e-flex e-con e-parent\" data-id=\"5a2cce4e\" data-element_type=\"container\">\n\t\t\t\t<div class=\"elementor-element elementor-element-7065ba76 elementor-invisible elementor-widget elementor-widget-elementskit-heading\" data-id=\"7065ba76\" data-element_type=\"widget\" data-settings=\"{&quot;_animation&quot;:&quot;fadeIn&quot;}\" data-widget_type=\"elementskit-heading.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<div class=\"ekit-wid-con\" ><div class=\"ekit-heading elementskit-section-title-wraper text_left   ekit_heading_tablet-   ekit_heading_mobile-\"><h1 class=\"ekit-heading--title elementskit-section-title\">Chaperonins<\/h1><div class=\"ekit_heading_separetor_wraper ekit_heading_elementskit-border-divider elementskit-style-long\"><div class=\"elementskit-border-divider elementskit-style-long\"><\/div><\/div><\/div><\/div>\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-5cb32fa0 e-flex e-con-boxed e-con e-parent\" data-id=\"5cb32fa0\" data-element_type=\"container\">\n\t\t\t\t\t<div class=\"e-con-inner\">\n\t\t\t\t<div class=\"elementor-element elementor-element-44940ad2 elementor-invisible elementor-widget elementor-widget-text-editor\" data-id=\"44940ad2\" data-element_type=\"widget\" data-settings=\"{&quot;_animation&quot;:&quot;fadeIn&quot;}\" data-widget_type=\"text-editor.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<style>\/*! elementor - v3.21.0 - 30-04-2024 *\/\n.elementor-widget-text-editor.elementor-drop-cap-view-stacked .elementor-drop-cap{background-color:#69727d;color:#fff}.elementor-widget-text-editor.elementor-drop-cap-view-framed .elementor-drop-cap{color:#69727d;border:3px solid;background-color:transparent}.elementor-widget-text-editor:not(.elementor-drop-cap-view-default) .elementor-drop-cap{margin-top:8px}.elementor-widget-text-editor:not(.elementor-drop-cap-view-default) .elementor-drop-cap-letter{width:1em;height:1em}.elementor-widget-text-editor .elementor-drop-cap{float:left;text-align:center;line-height:1;font-size:50px}.elementor-widget-text-editor .elementor-drop-cap-letter{display:inline-block}<\/style>\t\t\t\t<p class=\" translation-block\">Chaperonins are ubiquitous protein complexes that promote the proper folding of newly synthesized proteins and prevent the aggregation of denatured proteins using ATP energy. They are divided into group I (bacterial, mitochondrial, chloroplast chaperonins) and group II (archaeal and eukaryotic cytosolic variants). However, both of these groups do not include the newly discovered viral chaperonins.<\/p>\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-5c4ed732 e-con-full e-flex e-con e-parent\" data-id=\"5c4ed732\" data-element_type=\"container\">\n\t\t\t\t<div class=\"elementor-element elementor-element-18fa020b elementor-invisible elementor-widget elementor-widget-elementskit-heading\" data-id=\"18fa020b\" data-element_type=\"widget\" data-settings=\"{&quot;_animation&quot;:&quot;fadeIn&quot;}\" data-widget_type=\"elementskit-heading.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<div class=\"ekit-wid-con\" ><div class=\"ekit-heading elementskit-section-title-wraper text_left   ekit_heading_tablet-   ekit_heading_mobile-\"><h1 class=\"ekit-heading--title elementskit-section-title\">Selected publications on the topic<\/h1><\/div><\/div>\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-29bcaf90 e-con-full e-flex e-con e-parent\" data-id=\"29bcaf90\" data-element_type=\"container\">\n\t\t<div class=\"elementor-element elementor-element-3d39d87e e-con-full e-flex e-con e-child\" data-id=\"3d39d87e\" data-element_type=\"container\" data-settings=\"{&quot;animation&quot;:&quot;none&quot;,&quot;animation_tablet&quot;:&quot;none&quot;}\">\n\t\t\t\t<div class=\"elementor-element elementor-element-c839115 elementor-widget__width-inherit elementor-widget elementor-widget-elementskit-heading\" data-id=\"c839115\" data-element_type=\"widget\" data-widget_type=\"elementskit-heading.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<div class=\"ekit-wid-con\" ><div class=\"ekit-heading elementskit-section-title-wraper text_left   ekit_heading_tablet-   ekit_heading_mobile-\"><a href=\"https:\/\/doi.org\/10.1038\/s41598-021-97657-x\"><h3 class=\"ekit-heading--title elementskit-section-title\">Novel cryo-EM structure of an ADP-bound GroEL\u2013GroES complex<\/h3><\/a><h6 class=\"ekit-heading--subtitle elementskit-section-subtitle\">\n\t\t\t\t\t\tSofia S. Kudryavtseva, Evgeny B. Pichkur, Igor A. Yaroshevich, Aleksandra A. Mamchur, Irina S. Panina, Andrei V. Moiseenko, Olga S. Sokolova, Vladimir I. Muronetz &amp; Tatiana B. Stanishneva-Konovalova\n\t\t\t\t\t<\/h6><\/div><\/div>\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-fa5c67f e-con-full e-flex e-con e-child\" data-id=\"fa5c67f\" data-element_type=\"container\">\n\t\t\t\t<div class=\"elementor-element elementor-element-3594fbe elementor-widget__width-initial elementor-widget elementor-widget-text-editor\" data-id=\"3594fbe\" data-element_type=\"widget\" data-widget_type=\"text-editor.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t\t\t<p>The GroEL\u2013GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release. Structural methods helped to reveal several conformational states and provide more information about the chaperonin functional cycle. Here, using cryo-EM we resolved two nucleotide-bound structures of the bullet-shaped GroEL\u2013GroES<sub>1<\/sub> complex at 3.4\u00a0\u00c5 resolution. The main difference between them is the relative orientation of their apical domains. Both structures contain nucleotides in cis and trans GroEL rings; in contrast to previously reported bullet-shaped complexes where nucleotides were only present in the cis ring. Our results suggest that the bound nucleotides correspond to ADP, and that such a state appears at low ATP:ADP ratios. <a href=\"https:\/\/doi.org\/10.1038\/s41598-021-97657-x\">DOI<\/a><\/p>\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<div class=\"elementor-element elementor-element-46ee5f3 elementor-widget elementor-widget-image\" data-id=\"46ee5f3\" data-element_type=\"widget\" data-widget_type=\"image.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<style>\/*! elementor - v3.21.0 - 30-04-2024 *\/\n.elementor-widget-image{text-align:center}.elementor-widget-image a{display:inline-block}.elementor-widget-image a img[src$=\".svg\"]{width:48px}.elementor-widget-image img{vertical-align:middle;display:inline-block}<\/style>\t\t\t\t\t\t\t\t\t\t<img fetchpriority=\"high\" decoding=\"async\" width=\"1144\" height=\"1144\" src=\"https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/05\/groe.gif\" class=\"attachment-full size-full wp-image-1347\" alt=\"\" \/>\t\t\t\t\t\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-f5ad566 e-con-full e-flex e-con e-child\" data-id=\"f5ad566\" data-element_type=\"container\" data-settings=\"{&quot;animation&quot;:&quot;none&quot;,&quot;animation_tablet&quot;:&quot;none&quot;}\">\n\t\t\t\t<div class=\"elementor-element elementor-element-49e1e46 elementor-widget__width-inherit elementor-widget elementor-widget-elementskit-heading\" data-id=\"49e1e46\" data-element_type=\"widget\" data-widget_type=\"elementskit-heading.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<div class=\"ekit-wid-con\" ><div class=\"ekit-heading elementskit-section-title-wraper text_left   ekit_heading_tablet-   ekit_heading_mobile-\"><a href=\"https:\/\/doi.org\/10.1016\/j.jsb.2019.107439\"><h3 class=\"ekit-heading--title elementskit-section-title\">Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin<\/h3><\/a><h6 class=\"ekit-heading--subtitle elementskit-section-subtitle\">\n\t\t\t\t\t\tTatiana B. Stanishneva-Konovalova, Pavel I. Semenyuk, Lidia P. Kurochkina, Evgeny B. Pichkur, Alexander L. Vasilyev, Mikhail V. Kovalchuk, Mikhail P. Kirpichnikov, Olga S. Sokolova\n\t\t\t\t\t<\/h6><\/div><\/div>\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-878427f e-con-full e-flex e-con e-child\" data-id=\"878427f\" data-element_type=\"container\">\n\t\t\t\t<div class=\"elementor-element elementor-element-2cc30df elementor-widget__width-initial elementor-widget elementor-widget-text-editor\" data-id=\"2cc30df\" data-element_type=\"widget\" data-widget_type=\"text-editor.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t\t\t<p>Chaperonins are ubiquitously present protein complexes, which assist the proper folding of newly synthesized proteins and prevent aggregation of denatured proteins in an ATP-dependent manner. They are classified into group I (bacterial, mitochondrial, chloroplast chaperonins) and group II (archaeal and eukaryotic cytosolic variants). However, both of these groups do not include recently discovered viral chaperonins. Here, we solved the symmetry-free cryo-EM structures of a single-ring chaperonin encoded by the gene 246 of bacteriophage OBP <em>Pseudomonas fluorescens<\/em>, in the nucleotide-free, ATP\u03b3S-, and ADP-bound states, with resolutions of 4.3\u00a0\u00c5, 5.0\u00a0\u00c5, and 6\u00a0\u00c5, respectively. The structure of OBP chaperonin reveals a unique subunit arrangement, with three pairs of subunits and one unpaired subunit. Each pair combines subunits in two possible conformations, differing in nucleotide-binding affinity. The binding of nucleotides results in the increase of subunits\u2019 conformational variability. Due to its unique structural and functional features, OBP chaperonin can represent a new group. <a href=\"https:\/\/doi.org\/10.1016\/j.jsb.2019.107439\">DOI<\/a><\/p>\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<div class=\"elementor-element elementor-element-910ed16 elementor-widget elementor-widget-image\" data-id=\"910ed16\" data-element_type=\"widget\" data-widget_type=\"image.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t\t\t\t\t\t\t\t\t<img decoding=\"async\" width=\"1144\" height=\"1144\" src=\"https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/05\/obp.gif\" class=\"attachment-full size-full wp-image-1335\" alt=\"\" \/>\t\t\t\t\t\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-6d48633 e-con-full e-flex e-con e-child\" data-id=\"6d48633\" data-element_type=\"container\" data-settings=\"{&quot;animation&quot;:&quot;none&quot;,&quot;animation_tablet&quot;:&quot;none&quot;}\">\n\t\t\t\t<div class=\"elementor-element elementor-element-89c725d elementor-widget__width-inherit elementor-widget elementor-widget-elementskit-heading\" data-id=\"89c725d\" data-element_type=\"widget\" data-widget_type=\"elementskit-heading.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t<div class=\"ekit-wid-con\" ><div class=\"ekit-heading elementskit-section-title-wraper text_left   ekit_heading_tablet-   ekit_heading_mobile-\"><a href=\"https:\/\/doi.org\/10.3390\/biomedicines10102347\"><h3 class=\"ekit-heading--title elementskit-section-title\">Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis<\/h3><\/a><h6 class=\"ekit-heading--subtitle elementskit-section-subtitle\">\n\t\t\t\t\t\t Olga S. Sokolova, Evgeny B. Pichkur, Ekaterina S. Maslova, Lidia P. Kurochkina, Pavel I. Semenyuk, Petr V. Konarev, Valeriya R. Samygina, Tatiana B. Stanishneva-Konovalova\n\t\t\t\t\t<\/h6><\/div><\/div>\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-a728a97 e-con-full e-flex e-con e-child\" data-id=\"a728a97\" data-element_type=\"container\">\n\t\t\t\t<div class=\"elementor-element elementor-element-fe1cfca elementor-widget__width-initial elementor-widget elementor-widget-text-editor\" data-id=\"fe1cfca\" data-element_type=\"widget\" data-widget_type=\"text-editor.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t\t\t<p>Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and eukaryotes. Recently, chaperonins of a prospective new group were discovered in giant bacteriophages; however, structures have been determined for only two of them. Here, using cryo-EM, we resolved a structure of a new chaperonin encoded by gene 228 of phage AR9 <i>B. subtilis<\/i>. This structure has similarities and differences with members of both groups, as well as with other known phage chaperonins, which further proves their diversity. <a href=\"https:\/\/doi.org\/10.3390\/biomedicines10102347\">DOI<\/a><\/p>\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<div class=\"elementor-element elementor-element-9c5501a elementor-widget elementor-widget-image\" data-id=\"9c5501a\" data-element_type=\"widget\" data-widget_type=\"image.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t\t\t\t\t\t\t\t\t<img decoding=\"async\" width=\"1089\" height=\"787\" src=\"https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility.png\" class=\"attachment-full size-full wp-image-2978\" alt=\"\" srcset=\"https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility.png 1089w, https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility-300x217.png 300w, https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility-1024x740.png 1024w, https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility-768x555.png 768w, https:\/\/www.bioeng.ru\/structbiotech\/wp-content\/uploads\/sites\/3\/2024\/10\/local-flexibility-18x12.png 18w\" sizes=\"(max-width: 1089px) 100vw, 1089px\" \/>\t\t\t\t\t\t\t\t\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t<div class=\"elementor-element elementor-element-5b925348 e-flex e-con-boxed e-con e-parent\" data-id=\"5b925348\" data-element_type=\"container\">\n\t\t\t\t\t<div class=\"e-con-inner\">\n\t\t\t\t<div class=\"elementor-element elementor-element-38e0a719 elementor-align-center elementor-widget__width-initial elementor-widget elementor-widget-button\" data-id=\"38e0a719\" data-element_type=\"widget\" data-widget_type=\"button.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t<div class=\"elementor-button-wrapper\">\n\t\t\t<a class=\"elementor-button elementor-button-link elementor-size-sm\" href=\"https:\/\/www.bioeng.ru\/structbiotech\/en\/#directions\">\n\t\t\t\t\t\t<span class=\"elementor-button-content-wrapper\">\n\t\t\t\t\t\t\t\t\t<span class=\"elementor-button-text\">Other research directions<\/span>\n\t\t\t\t\t<\/span>\n\t\t\t\t\t<\/a>\n\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<div class=\"elementor-element elementor-element-13c63546 elementor-align-center elementor-widget__width-initial elementor-widget elementor-widget-button\" data-id=\"13c63546\" data-element_type=\"widget\" data-widget_type=\"button.default\">\n\t\t\t\t<div class=\"elementor-widget-container\">\n\t\t\t\t\t<div class=\"elementor-button-wrapper\">\n\t\t\t<a class=\"elementor-button elementor-button-link elementor-size-sm\" href=\"https:\/\/www.bioeng.ru\/structbiotech\/en\/articles\/\">\n\t\t\t\t\t\t<span class=\"elementor-button-content-wrapper\">\n\t\t\t\t\t\t\t\t\t<span class=\"elementor-button-text\">All publications of the group<\/span>\n\t\t\t\t\t<\/span>\n\t\t\t\t\t<\/a>\n\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t\t<\/div>\n\t\t\t\t<\/div>\n\t\t\t\t<\/div>","protected":false},"excerpt":{"rendered":"<p>\u0428\u0430\u043f\u0435\u0440\u043e\u043d\u0438\u043d\u044b \u0428\u0430\u043f\u0435\u0440\u043e\u043d\u0438\u043d\u044b \u2014 \u044d\u0442\u043e \u043f\u043e\u0432\u0441\u0435\u043c\u0435\u0441\u0442\u043d\u043e \u043f\u0440\u0438\u0441\u0443\u0442\u0441\u0442\u0432\u0443\u044e\u0449\u0438\u0435 \u0431\u0435\u043b\u043a\u043e\u0432\u044b\u0435 \u043a\u043e\u043c\u043f\u043b\u0435\u043a\u0441\u044b, \u043a\u043e\u0442\u043e\u0440\u044b\u0435 \u0441\u043f\u043e\u0441\u043e\u0431\u0441\u0442\u0432\u0443\u044e\u0442 \u043f\u0440\u0430\u0432\u0438\u043b\u044c\u043d\u043e\u043c\u0443 \u0441\u0432\u043e\u0440\u0430\u0447\u0438\u0432\u0430\u043d\u0438\u044e 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