6t1w
From Proteopedia
(Difference between revisions)
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==Structure of E. coli BamA in complex with lipoprotein RcsF== | ==Structure of E. coli BamA in complex with lipoprotein RcsF== | ||
| - | <StructureSection load='6t1w' size='340' side='right'caption='[[6t1w]]' scene=''> | + | <StructureSection load='6t1w' size='340' side='right'caption='[[6t1w]], [[Resolution|resolution]] 3.79Å' 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=6T1W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T1W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t1w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T1W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T1W FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1w OCA], [http://pdbe.org/6t1w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t1w RCSB], [http://www.ebi.ac.uk/pdbsum/6t1w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1w ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bamA, yaeT, yzzN, yzzY, b0177, JW0172 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1w OCA], [http://pdbe.org/6t1w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t1w RCSB], [http://www.ebi.ac.uk/pdbsum/6t1w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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/E2QFC4_ECOLX E2QFC4_ECOLX]] Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects.[HAMAP-Rule:MF_00976] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The beta-barrel assembly machinery (BAM) inserts outer membrane beta-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assembling RcsF-OMP complexes. Here, we report the crystal structure of the key BAM component BamA in complex with RcsF. BamA adopts an inward-open conformation, with the lateral gate to the membrane closed. RcsF is lodged deep within the lumen of the BamA barrel, binding regions proposed to undergo outward and lateral opening during OMP insertion. On the basis of our structural and biochemical data, we propose a push-and-pull model for RcsF export following conformational cycling of BamA, and provide a mechanistic explanation for how RcsF uses its interaction with BamA to detect envelope stress. Our data also suggest that the flux of incoming OMP substrates is involved in the control of BAM activity. | ||
| + | |||
| + | Structural insight into the formation of lipoprotein-beta-barrel complexes.,Rodriguez-Alonso R, Letoquart J, Nguyen VS, Louis G, Calabrese AN, Iorga BI, Radford SE, Cho SH, Remaut H, Collet JF Nat Chem Biol. 2020 Jun 22. pii: 10.1038/s41589-020-0575-0. doi:, 10.1038/s41589-020-0575-0. PMID:32572278<ref>PMID:32572278</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6t1w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecoli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Collet | + | [[Category: Collet, J F]] |
| - | [[Category: Letoquart J]] | + | [[Category: Letoquart, J]] |
| - | [[Category: Remaut H]] | + | [[Category: Remaut, H]] |
| + | [[Category: Beta barrel assembly]] | ||
| + | [[Category: Lipoprotein]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Stress response]] | ||
Revision as of 11:31, 22 July 2020
Structure of E. coli BamA in complex with lipoprotein RcsF
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