{"id":955,"date":"2026-04-15T12:58:17","date_gmt":"2026-04-15T12:58:17","guid":{"rendered":"https:\/\/citations.tools.bio-logic.fr\/?p=955"},"modified":"2026-04-15T12:58:17","modified_gmt":"2026-04-15T12:58:17","slug":"allosteric-signalling-in-the-outer-membrane-translocation-domain-of-papc-usher","status":"publish","type":"post","link":"https:\/\/citations.tools.bio-logic.fr\/?p=955","title":{"rendered":"Allosteric signalling in the outer membrane translocation domain of PapC usher"},"content":{"rendered":"<h4>DOI:<\/h4>\n<p><a href=\"https:\/\/doi.org\/10.7554\/elife.03532\" target=\"_blank\" rel=\"noopener\">10.7554\/elife.03532<\/a><\/p>\n<h4>Authors:<\/h4>\n<p>Irene Farabella, Thieng Pham, Nadine S. Henderson, Sebastian Geibel, Gilles Phan, David G. Thanassi, Anne H. Delcour, Gabriel Waksman, Maya Topf<\/p>\n<h4>Abstract:<\/h4>\n<p>PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large \u03b2-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits across the membrane. Previous studies suggested that this gating mechanism is controlled by a \u03b2-hairpin and an \u03b1-helix. To investigate the role of these elements in allosteric signal communication, we developed a method combining evolutionary and molecular dynamics studies of the native translocation domain and mutants lacking the \u03b2-hairpin and\/or the \u03b1-helix. Analysis of a hybrid residue interaction network suggests distinct regions (residue &lsquo;communities&rsquo;) within the translocation domain (especially around \u03b212-\u03b214) linking these elements, thereby modulating PapC gating. Antibiotic sensitivity and electrophysiology experiments on a set of alanine-substitution mutants confirmed functional roles for four of these communities. This study illuminates the gating mechanism of PapC ushers and its importance in maintaining outer-membrane permeability.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>DOI: 10.7554\/elife.03532 Authors: Irene Farabella, Thieng Pham, Nadine S. Henderson, Sebastian Geibel, Gilles Phan, David G. Thanassi, Anne H. Delcour, Gabriel Waksman, Maya Topf Abstract: PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large \u03b2-barrel occluded by a plug domain, which is [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[11],"tags":[],"class_list":["post-955","post","type-post","status-publish","format-standard","hentry","category-m-470-ac-dc-sds"],"_links":{"self":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/955","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=955"}],"version-history":[{"count":0,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/955\/revisions"}],"wp:attachment":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=955"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=955"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=955"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}