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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/"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> | + | <table><tr><td colspan='2'>[[4k3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_ducreyi Haemophilus ducreyi]. 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 [https://proteopedia.org/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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k3c OCA], [https://pdbe.org/4k3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k3c RCSB], [https://www.ebi.ac.uk/pdbsum/4k3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k3c ProSAT]</span></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 "Bacillus ulceris cancrosi" Kruse 1896])</td></tr>
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| - | <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 == |
| - | [[http://www.uniprot.org/uniprot/Q93PM2_HAEDC 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] | + | [https://www.uniprot.org/uniprot/Q93PM2_HAEDC 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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Bam complex|Bam complex]] | + | *[[Bam complex 3D structures|Bam complex 3D structures]] |
| | + | *[[Insertase|Insertase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus ulceris cancrosi kruse 1896]] | + | [[Category: Large Structures]] |
| - | [[Category: Buchanan, S K]] | + | [[Category: Buchanan SK]] |
| - | [[Category: Chang, H]] | + | [[Category: Chang H]] |
| - | [[Category: Easley, N]] | + | [[Category: Easley N]] |
| - | [[Category: Lukacik, P]] | + | [[Category: Lukacik P]] |
| - | [[Category: Noinaj, N]] | + | [[Category: Noinaj N]] |
| - | [[Category: Beta-barrel membrane protein]]
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| - | [[Category: Insertase]]
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| - | [[Category: Membrane protein]]
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| 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 PubMed
beta-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 Also
References
- ↑ Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, Buchanan SK. Structural insight into the biogenesis of beta-barrel membrane proteins. Nature. 2013 Sep 1. doi: 10.1038/nature12521. PMID:23995689 doi:10.1038/nature12521
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