{"id":3264,"date":"2020-06-08T20:51:14","date_gmt":"2020-06-08T19:51:14","guid":{"rendered":"https:\/\/ibb.uab.cat\/?p=3264"},"modified":"2020-06-08T21:00:55","modified_gmt":"2020-06-08T20:00:55","slug":"molecular-biology-structure-and-mechanism-of-the-nap-adhesion-complex-from-the-human-pathogen-mycoplasma-genitalium","status":"publish","type":"post","link":"https:\/\/ibb.uab.cat\/index.php\/2020\/06\/08\/molecular-biology-structure-and-mechanism-of-the-nap-adhesion-complex-from-the-human-pathogen-mycoplasma-genitalium\/","title":{"rendered":"Molecular Biology &#8220;Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium&#8221;"},"content":{"rendered":"<p><img loading=\"lazy\" class=\"wp-image-3265 alignleft\" src=\"https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1.jpg\" alt=\"\" width=\"581\" height=\"769\" srcset=\"https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1.jpg 1784w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1-227x300.jpg 227w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1-768x1016.jpg 768w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1-774x1024.jpg 774w, https:\/\/ibb.uab.cat\/wp-content\/uploads\/biologia-molecular-1-197x260.jpg 197w\" sizes=\"(max-width: 581px) 100vw, 581px\" \/><a href=\"https:\/\/www.nature.com\/articles\/s41467-020-16511-2\" target=\"_blank\" rel=\"noopener\">https:\/\/www.nature.com\/articles\/s41467-020-16511-2<\/a><\/p>\n<h2 id=\"Abs1\" class=\"c-article-section__title js-section-title js-c-reading-companion-sections-item\">Abstract<\/h2>\n<div id=\"Abs1-content\" class=\"c-article-section__content\">\n<p style=\"text-align: justify;\"><i>Mycoplasma genitalium<\/i>\u00a0is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9.8 and 15\u2009\u00c5, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of\u00a0<i>M. genitalium<\/i>\u00a0to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity.<\/p>\n<\/div>\n<p>&nbsp;<\/p>\n<p><strong>Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium. Aparicio et al.\u00a0<em>Nature communications,<\/em>\u00a0doi: 10.1038\/s41467-020-16511-2\u00a0<a href=\"https:\/\/www.nature.com\/articles\/s41467-020-16511-2\">https:\/\/www.nature.com\/articles\/s41467-020-16511-2<\/a><\/strong><\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>https:\/\/www.nature.com\/articles\/s41467-020-16511-2 Abstract Mycoplasma genitalium\u00a0is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. [&hellip;]<\/p>\n","protected":false},"author":65,"featured_media":2912,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[4],"tags":[],"_links":{"self":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3264"}],"collection":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/users\/65"}],"replies":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/comments?post=3264"}],"version-history":[{"count":4,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3264\/revisions"}],"predecessor-version":[{"id":3269,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/3264\/revisions\/3269"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media\/2912"}],"wp:attachment":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media?parent=3264"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/categories?post=3264"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/tags?post=3264"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}