5ljo

From Proteopedia

(Difference between revisions)

Current revision

E. coli BAM complex (BamABCDE) by cryoEM

5ljo, resolution 4.90Å

Structural highlights

5ljo is a 5 chain structure with sequence from Escherichia coli and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4.9Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hagan CL, Kim S, Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr, 8. PMID:20378773 doi:10.1126/science.1188919
↑ Hagan CL, Kahne D. The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly. Biochemistry. 2011 Sep 6;50(35):7444-6. doi: 10.1021/bi2010784. Epub 2011 Aug 11. PMID:21823654 doi:10.1021/bi2010784
↑ Albrecht R, Zeth K. Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem. 2011 Aug 5;286(31):27792-803. Epub 2011 May 17. PMID:21586578 doi:10.1074/jbc.M111.238931
↑ Noinaj N, Fairman JW, Buchanan SK. The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex. J Mol Biol. 2011 Jan 26. PMID:21277859 doi:10.1016/j.jmb.2011.01.042
↑ Iadanza MG, Higgins AJ, Schiffrin B, Calabrese AN, Brockwell DJ, Ashcroft AE, Radford SE, Ranson NA. Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM. Nat Commun. 2016 Sep 30;7:12865. doi: 10.1038/ncomms12865. PMID:27686148 doi:http://dx.doi.org/10.1038/ncomms12865

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ljo"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ljo is ON HOLD
+==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>
+</table>
+== 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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ljo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Bam complex 3D structures|Bam complex 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[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]]

5ljo

From Proteopedia

Current revision

E. coli BAM complex (BamABCDE) by cryoEM

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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