View source for 5ljo


==E. coli BAM complex (BamABCDE) by cryoEM==
<SX load='5ljo' size='340' side='right' viewer='molstar' caption='[[5ljo]], [[Resolution|resolution]] 4.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ljo]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LJO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.9&#8491;</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=5ljo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ljo OCA], [https://pdbe.org/5ljo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ljo RCSB], [https://www.ebi.ac.uk/pdbsum/5ljo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ljo ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/BAMB_ECOLI BAMB_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, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:21586578</ref> <ref>PMID:21277859</ref> 
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== Publication Abstract from PubMed ==
The beta-barrel assembly machinery (BAM) is a approximately 203 kDa complex of five proteins (BamA-E), which is essential for viability in E. coli. BAM promotes the folding and insertion of beta-barrel proteins into the outer membrane via a poorly understood mechanism. Several current models suggest that BAM functions through a 'lateral gating' motion of the beta-barrel of BamA. Here we present a cryo-EM structure of the BamABCDE complex, at 4.9 A resolution. The structure is in a laterally open conformation showing that gating is independent of BamB binding. We describe conformational changes throughout the complex and interactions between BamA, B, D and E, and the detergent micelle that suggest communication between BAM and the lipid bilayer. Finally, using an enhanced reconstitution protocol and functional assays, we show that for the outer membrane protein OmpT, efficient folding in vitro requires lateral gating in BAM.

Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM.,Iadanza MG, Higgins AJ, Schiffrin B, Calabrese AN, Brockwell DJ, Ashcroft AE, Radford SE, Ranson NA Nat Commun. 2016 Sep 30;7:12865. doi: 10.1038/ncomms12865. PMID:27686148<ref>PMID:27686148</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ljo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bam complex 3D structures|Bam complex 3D structures]]
== References ==
<references/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Ashcroft AE]]
[[Category: Brockwell DJ]]
[[Category: Calabrese AN]]
[[Category: Higgins AJ]]
[[Category: Iadanza MG]]
[[Category: Radford SE]]
[[Category: Ranson NA]]
[[Category: Schffrin B]]