5ekq
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==The structure of the BamACDE subcomplex from E. coli== |
| + | <StructureSection load='5ekq' size='340' side='right' caption='[[5ekq]], [[Resolution|resolution]] 3.39Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ekq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EKQ FirstGlance]. <br> | ||
| + | </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=5ekq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ekq OCA], [http://pdbe.org/5ekq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ekq RCSB], [http://www.ebi.ac.uk/pdbsum/5ekq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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/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> [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | beta-Barrel outer membrane proteins (OMPs) are found in the outer membranes of Gram-negative bacteria and are essential for nutrient import, signaling, and adhesion. A 200-kilodalton five-component complex called the beta-barrel assembly machinery (BAM) complex has been implicated in the biogenesis of OMPs. We report the structure of the BAM complex from Escherichia coli, revealing that binding of BamCDE modulates the conformation of BamA, the central component, which may serve to regulate the BAM complex. The periplasmic domain of BamA was in a closed state that prevents access to the barrel lumen, which indicates substrate OMPs may not be threaded through the barrel during biogenesis. Further, conformational shifts in the barrel domain lead to opening of the exit pore and rearrangement at the lateral gate. | ||
| - | The | + | The structure of the beta-barrel assembly machinery complex.,Bakelar J, Buchanan SK, Noinaj N Science. 2016 Jan 8;351(6269):180-6. doi: 10.1126/science.aad3460. PMID:26744406<ref>PMID:26744406</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ekq" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bakelar, J]] | [[Category: Bakelar, J]] | ||
| + | [[Category: Buchanan, S K]] | ||
[[Category: Noinaj, N]] | [[Category: Noinaj, N]] | ||
| + | [[Category: Beta-barrel]] | ||
| + | [[Category: Insertase]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Outer membrane protein]] | ||
Revision as of 17:01, 20 January 2016
The structure of the BamACDE subcomplex from E. coli
| |||||||||||
