7tt1: Difference between revisions
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==== | ==BamABCDE bound to substrate EspP class 4== | ||
<StructureSection load='7tt1' size='340' side='right'caption='[[7tt1]]' scene=''> | <StructureSection load='7tt1' size='340' side='right'caption='[[7tt1]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tt1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TT1 FirstGlance]. <br> | ||
</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=7tt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tt1 OCA], [https://pdbe.org/7tt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7tt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tt1 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]] 4.3Å</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=7tt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tt1 OCA], [https://pdbe.org/7tt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tt1 RCSB], [https://www.ebi.ac.uk/pdbsum/7tt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tt1 ProSAT]</span></td></tr> | |||
</table> | </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 == | |||
Transmembrane beta barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the beta barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. Here, we used single-particle cryo-EM to visualize the folding dynamics of a model beta barrel protein (EspP) by BAM. We found that BAM binds the highly conserved "beta signal" motif of EspP to correctly orient beta strands in the OM during folding. We also found that the folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated beta sheets are attached to the essential BAM subunit, BamA. The structures show an unprecedented deflection of the membrane surrounding the EspP intermediates and suggest that beta sheets progressively fold toward BamA to form a beta barrel. Along with in vivo experiments that tracked beta barrel folding while the OM tension was modified, our results support a model in which BAM harnesses OM elasticity to accelerate beta barrel folding. | |||
Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.,Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, Bernstein HD Cell. 2022 Mar 31;185(7):1143-1156.e13. doi: 10.1016/j.cell.2022.02.016. Epub , 2022 Mar 15. PMID:35294859<ref>PMID:35294859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7tt1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bam complex 3D structures|Bam complex 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bernstein HD]] | ||
[[Category: Dowdy T]] | |||
[[Category: Doyle MT]] | |||
[[Category: Hinshaw JE]] | |||
[[Category: Jimah JR]] | |||
[[Category: Larion M]] | |||
[[Category: Ohlemacher SI]] | |||
Latest revision as of 17:04, 6 November 2024
BamABCDE bound to substrate EspP class 4BamABCDE bound to substrate EspP class 4
Structural highlights
FunctionBAMB_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 PubMedTransmembrane beta barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the beta barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. Here, we used single-particle cryo-EM to visualize the folding dynamics of a model beta barrel protein (EspP) by BAM. We found that BAM binds the highly conserved "beta signal" motif of EspP to correctly orient beta strands in the OM during folding. We also found that the folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated beta sheets are attached to the essential BAM subunit, BamA. The structures show an unprecedented deflection of the membrane surrounding the EspP intermediates and suggest that beta sheets progressively fold toward BamA to form a beta barrel. Along with in vivo experiments that tracked beta barrel folding while the OM tension was modified, our results support a model in which BAM harnesses OM elasticity to accelerate beta barrel folding. Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.,Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, Bernstein HD Cell. 2022 Mar 31;185(7):1143-1156.e13. doi: 10.1016/j.cell.2022.02.016. Epub , 2022 Mar 15. PMID:35294859[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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