4k3c: Difference between revisions
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==The crystal structure of BamA from Haemophilus ducreyi lacking POTRA domains 1-3== | ==The crystal structure of BamA from Haemophilus ducreyi lacking POTRA domains 1-3== | ||
<StructureSection load='4k3c' size='340' side='right' caption='[[4k3c]], [[Resolution|resolution]] 2.91Å' scene=''> | <StructureSection load='4k3c' size='340' side='right' caption='[[4k3c]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4k3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4k3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_ulceris_cancrosi"_kruse_1896 "bacillus ulceris cancrosi" kruse 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K3C FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k3b|4k3b]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k3b|4k3b]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D15, bamA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=730 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D15, bamA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=730 "Bacillus ulceris cancrosi" Kruse 1896])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k3c RCSB], [http://www.ebi.ac.uk/pdbsum/4k3c PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k3c OCA], [http://pdbe.org/4k3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k3c RCSB], [http://www.ebi.ac.uk/pdbsum/4k3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k3c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4k3c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bam complex|Bam complex]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus ulceris cancrosi kruse 1896]] | ||
[[Category: Buchanan, S K]] | [[Category: Buchanan, S K]] | ||
[[Category: Chang, H]] | [[Category: Chang, H]] | ||
Revision as of 13:55, 4 August 2016
The crystal structure of BamA from Haemophilus ducreyi lacking POTRA domains 1-3The crystal structure of BamA from Haemophilus ducreyi lacking POTRA domains 1-3
Structural highlights
Function[Q93PM2_HAEDC] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (By similarity).[HAMAP-Rule:MF_01430] Publication Abstract from PubMedbeta-barrel membrane proteins are essential for nutrient import, signalling, motility and survival. In Gram-negative bacteria, the beta-barrel assembly machinery (BAM) complex is responsible for the biogenesis of beta-barrel membrane proteins, with homologous complexes found in mitochondria and chloroplasts. Here we describe the structure of BamA, the central and essential component of the BAM complex, from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi. BamA consists of a large periplasmic domain attached to a 16-strand transmembrane beta-barrel domain. Three structural features shed light on the mechanism by which BamA catalyses beta-barrel assembly. First, the interior cavity is accessible in one BamA structure and conformationally closed in the other. Second, an exterior rim of the beta-barrel has a distinctly narrowed hydrophobic surface, locally destabilizing the outer membrane. And third, the beta-barrel can undergo lateral opening, suggesting a route from the interior cavity in BamA into the outer membrane. Structural insight into the biogenesis of beta-barrel membrane proteins.,Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, Buchanan SK Nature. 2013 Sep 1. doi: 10.1038/nature12521. PMID:23995689[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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