5d0q

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'''Unreleased structure'''
 
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The entry 5d0q is ON HOLD
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==BamACDE complex, outer membrane beta-barrel assembly machinery (BAM) complex==
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<StructureSection load='5d0q' size='340' side='right' caption='[[5d0q]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5d0q]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D0Q FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d0o|5d0o]]</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=5d0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d0q OCA], [http://pdbe.org/5d0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d0q RCSB], [http://www.ebi.ac.uk/pdbsum/5d0q PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/BAME_ECOLI BAME_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.<ref>PMID:17404237</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> <ref>PMID:21207987</ref> <ref>PMID:21586578</ref> [[http://www.uniprot.org/uniprot/BAMA_ECOLI BAMA_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> [[http://www.uniprot.org/uniprot/BAMD_ECOLI BAMD_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions.[HAMAP-Rule:MF_00922]<ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21586578</ref> <ref>PMID:21823654</ref> <ref>PMID:22281737</ref> [[http://www.uniprot.org/uniprot/BAMC_ECOLI BAMC_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD.[HAMAP-Rule:MF_00924]<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the beta-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB-BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane beta-barrel of BamA to induce movement of the beta-strands of the barrel and promote insertion of the nascent OMP.
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Authors: Gu, Y., Paterson, N., Zeng, Y., Dong, H., Wang, W., Dong, C.
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Structural basis of outer membrane protein insertion by the BAM complex.,Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld PJ, Wang Z, Zhang Y, Wang W, Dong C Nature. 2016 Mar 3;531(7592):64-9. doi: 10.1038/nature17199. Epub 2016 Feb 22. PMID:26901871<ref>PMID:26901871</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Wang, W]]
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<div class="pdbe-citations 5d0q" style="background-color:#fffaf0;"></div>
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[[Category: Dong, H]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Dong, C]]
[[Category: Dong, C]]
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[[Category: Zeng, Y]]
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[[Category: Dong, H]]
[[Category: Gu, Y]]
[[Category: Gu, Y]]
[[Category: Paterson, N]]
[[Category: Paterson, N]]
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[[Category: Wang, W]]
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[[Category: Zeng, Y]]
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[[Category: E coli]]
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[[Category: Outer membrane beta-barrel assembly machinery complex]]
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[[Category: Outer membrane biogenesis]]
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[[Category: Outer membrane insertion]]
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[[Category: Protein transport]]

Revision as of 03:36, 10 March 2016

BamACDE complex, outer membrane beta-barrel assembly machinery (BAM) complex

5d0q, resolution 3.50Å

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