{"id":178,"date":"2006-03-26T00:47:24","date_gmt":"2006-03-26T00:47:24","guid":{"rendered":"http:\/\/alectos.com\/content\/?p=178"},"modified":"2006-03-26T00:47:24","modified_gmt":"2006-03-26T00:47:24","slug":"structure-bacterial-oga-homologue","status":"publish","type":"post","link":"https:\/\/alectos.com\/alectos-content\/index.php\/2006\/03\/26\/structure-bacterial-oga-homologue\/","title":{"rendered":"Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity"},"content":{"rendered":"<p>O-GlcNAc is an abundant post-translational modification of serine and threonine residues of nucleocytoplasmic proteins. This modification, found only within higher eukaryotes, is a dynamic modification that is often reciprocal to phosphorylation. In a manner analogous to phosphatases, a glycoside hydrolase termed O-GlcNAcase cleaves O-GlcNAc from modified proteins. Enzymes with high sequence similarity to human O-GlcNAcase are also found in human pathogens and symbionts. We report the three-dimensional structure of O-GlcNAcase from the human gut symbiont Bacteroides thetaiotaomicron both in its native form and in complex with a mimic of the reaction intermediate. Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual \u2018substrate-assisted\u2019 catalytic mechanism, which will inform the rational design of enzyme inhibitors.<\/p>\n<p>Source: <a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16565725\" target=\"_blank\" rel=\"noopener\">Dennis, R.J. et al. <em>Nat Struct Mol Biol<\/em> <strong>13<\/strong>, 365-71 (2006).<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>O-GlcNAc is an abundant post-translational modification of serine and threonine  [&#8230;]<\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"footnotes":""},"categories":[19],"tags":[18,20],"class_list":["post-178","post","type-post","status-publish","format-standard","hentry","category-publications","tag-oga","tag-sfu"],"_links":{"self":[{"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/posts\/178","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/comments?post=178"}],"version-history":[{"count":0,"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/posts\/178\/revisions"}],"wp:attachment":[{"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/media?parent=178"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/categories?post=178"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/alectos.com\/alectos-content\/index.php\/wp-json\/wp\/v2\/tags?post=178"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}