5ljo: Difference between revisions

Latest revision as of 18:30, 18 October 2023

E. coli BAM complex (BamABCDE) by cryoEM

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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
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:https://dx.doi.org/10.1038/ncomms12865

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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:https://dx.doi.org/10.1038/ncomms12865

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[5]

@@ Line 1: / Line 1: @@
 ==E. coli BAM complex (BamABCDE) by cryoEM==
-<StructureSection load='5ljo' size='340' side='right' caption='[[5ljo]], [[Resolution|resolution]] 4.90&Aring;' scene=''>
+<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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LJO FirstGlance]. <br>
+<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='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=5ljo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ljo OCA], [http://pdbe.org/5ljo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ljo RCSB], [http://www.ebi.ac.uk/pdbsum/5ljo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ljo ProSAT]</span></td></tr>
+</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 ==
-[[http://www.uniprot.org/uniprot/BAME_ECOL6 BAME_ECOL6]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. [[http://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>  [[http://www.uniprot.org/uniprot/BAMD_ECO57 BAMD_ECO57]] 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. [[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/BAMA_ECO45 BAMA_ECO45]] 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.[HAMAP-Rule:MF_01430]
+[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 ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 5ljo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Bam complex 3D structures|Bam complex 3D structures]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Ashcroft, A E]]
+[[Category: Escherichia coli]]
-[[Category: Brockwell, D J]]
+[[Category: Escherichia coli K-12]]
-[[Category: Calabrese, A N]]
+[[Category: Large Structures]]
-[[Category: Higgins, A J]]
+[[Category: Ashcroft AE]]
-[[Category: Iadanza, M G]]
+[[Category: Brockwell DJ]]
-[[Category: Radford, S E]]
+[[Category: Calabrese AN]]
-[[Category: Ranson, N A]]
+[[Category: Higgins AJ]]
-[[Category: Schffrin, B]]
+[[Category: Iadanza MG]]
-[[Category: Bam]]
+[[Category: Radford SE]]
-[[Category: Beta barrel]]
+[[Category: Ranson NA]]
-[[Category: Gram negative]]
+[[Category: Schffrin B]]
-[[Category: Membrane protein]]
-[[Category: Omp]]
-[[Category: Outer membrane]]

5ljo: Difference between revisions

Latest revision as of 18:30, 18 October 2023

E. coli BAM complex (BamABCDE) by cryoEM

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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