{"id":223,"date":"2017-10-31T13:36:08","date_gmt":"2017-10-31T17:36:08","guid":{"rendered":"https:\/\/health.uconn.edu\/structural-biology\/?page_id=223"},"modified":"2017-11-03T15:47:38","modified_gmt":"2017-11-03T19:47:38","slug":"topological-specificity-domain-of-mine","status":"publish","type":"page","link":"https:\/\/health.uconn.edu\/structural-biology\/protein-structures\/topological-specificity-domain-of-mine\/","title":{"rendered":"Topological Specificity Domain of MinE"},"content":{"rendered":"<div id=\"pl-223\"  class=\"panel-layout\" ><div id=\"pg-223-0\"  class=\"panel-grid panel-no-style\" ><div id=\"pgc-223-0-0\"  class=\"panel-grid-cell\" ><div id=\"panel-223-0-0-0\" class=\"so-panel widget widget_black-studio-tinymce widget_black_studio_tinymce panel-first-child panel-last-child\" data-index=\"0\" ><div class=\"textwidget\"><p><div style=\"width: 400px;\" class=\"wp-video\"><!--[if lt IE 9]><script>document.createElement('video');<\/script><![endif]-->\n<video class=\"wp-video-shortcode\" id=\"video-223-1\" width=\"400\" height=\"360\" loop=\"1\" autoplay=\"1\" preload=\"metadata\" controls=\"controls\"><source type=\"video\/mp4\" src=\"https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Topological-Mine-1.mp4?_=1\" \/><a href=\"https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Topological-Mine-1.mp4\">https:\/\/health.uconn.edu\/structural-biology\/wp-content\/uploads\/sites\/177\/2017\/11\/Topological-Mine-1.mp4<\/a><\/video><\/div><\/p>\n<\/div><\/div><\/div><div id=\"pgc-223-0-1\"  class=\"panel-grid-cell\" ><div class=\"panel-cell-style panel-cell-style-for-223-0-1\" ><div id=\"panel-223-0-1-0\" class=\"so-panel widget widget_black-studio-tinymce widget_black_studio_tinymce panel-first-child panel-last-child\" data-index=\"1\" ><div class=\"textwidget\"><p>Placement of the division septum in\u00a0<em>E. coli<\/em>\u00a0is negatively regulated by the three proteins encoded by the minBoperon: MinC, MinD, and MinE. MinC and MinD act in concert to form a global division inhibitor whose activity is restricted to polar sites by MinE. In the presence of MinE all three proteins undergo a bipolar oscillation that causes the time-averaged concentration of MinCD to be lowest at midcell, the preferred division site. The MinE topological specificity domain forms a novel absandwich in which two a helices lie atop a four-strandedb sheet. Mutation of the a-face residues shown in red causes a defect in MinCD oscillation with a resultant decrease in the topological fidelity of cell division.<\/p>\n<hr \/>\n<p>King, G.F., Shih, Y.-L., Maciejewski, M.W., Bains, N.P.S., Pan, B., Rowland, S.L., Mullen, G.P. and Rothfield, L.I. (2000) Structural basis for the topological specificity function of MinE.\u00a0<em>Nature Structural Biology<\/em>\u00a07, 1013-1017.<\/p>\n<p><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/entrez\/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;list_uids=11062554&amp;dopt=Abstract\">PubMed<\/a>\u00a0|\u00a0<a href=\"http:\/\/www.nature.com\/cgi-taf\/DynaPage.taf?file=\/nsb\/journal\/v7\/n11\/abs\/nsb1100_1013.html&amp;dynoptions=doi1035925536\" class=\"broken_link\">Journal<\/a>\u00a0|\u00a0<a href=\"http:\/\/www.nature.com\/cgi-taf\/DynaPage.taf?file=\/nsb\/journal\/v7\/n11\/full\/nsb1100_997.html\" class=\"broken_link\">News &amp; Views<\/a>\u00a0|\u00a0<a href=\"http:\/\/www.rcsb.org\/pdb\/cgi\/explore.cgi?pid=281731037807968&amp;pdbId=1EV0\" class=\"broken_link\">PDB Link<\/a><\/p>\n<p><a href=\"https:\/\/health.uconn.edu\/structural-biology\/protein-structures\/\">Back to Image Gallery<\/a><\/p>\n<\/div><\/div><\/div><\/div><\/div><\/div>","protected":false},"excerpt":{"rendered":"<p>Placement of the division septum in\u00a0E. coli\u00a0is negatively regulated by the three proteins encoded by the minBoperon: MinC, MinD, and MinE. MinC and MinD act in concert to form a global division inhibitor whose activity is restricted to polar sites by MinE. In the presence of MinE all three proteins undergo a bipolar oscillation that [&hellip;]<\/p>\n","protected":false},"author":38,"featured_media":0,"parent":155,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"acf":[],"publishpress_future_action":{"enabled":false,"date":"2026-04-27 21:53:39","action":"change-status","newStatus":"draft","terms":[],"taxonomy":""},"_links":{"self":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/223"}],"collection":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/users\/38"}],"replies":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/comments?post=223"}],"version-history":[{"count":6,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/223\/revisions"}],"predecessor-version":[{"id":564,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/223\/revisions\/564"}],"up":[{"embeddable":true,"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/pages\/155"}],"wp:attachment":[{"href":"https:\/\/health.uconn.edu\/structural-biology\/wp-json\/wp\/v2\/media?parent=223"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}