7ye4: Difference between revisions
New page: '''Unreleased structure''' The entry 7ye4 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==BAM-EspP complex structure with BamA-G431C and G781C/EspP-N1293C and A1043C mutations in nanodisc== | ||
<StructureSection load='7ye4' size='340' side='right'caption='[[7ye4]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ye4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YE4 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]] 3.4Å</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=7ye4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ye4 OCA], [https://pdbe.org/7ye4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ye4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ye4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ye4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane beta-barrel proteins (OMPs) that are essential interchange portals of materials(1-3). All known OMPs share the antiparallel beta-strand topology(4), implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial beta-barrel assembly machinery (BAM) to initiate OMP folding(5,6); however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly. | |||
Structural basis of BAM-mediated outer membrane beta-barrel protein assembly.,Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, Dong H Nature. 2023 May;617(7959):185-193. doi: 10.1038/s41586-023-05988-8. Epub 2023 , Apr 26. PMID:37100902<ref>PMID:37100902</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ye4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Escherichia coli O157:H7]] | |||
[[Category: Large Structures]] | |||
[[Category: Chang S]] | |||
[[Category: Dong C]] | |||
[[Category: Dong H]] | |||
[[Category: Lu G]] | |||
[[Category: Luo B]] | |||
[[Category: Luo Q]] | |||
[[Category: Shen C]] | |||
[[Category: Tang X]] | |||
[[Category: Wei X]] | |||
[[Category: Zhang X]] | |||
[[Category: Zhang Z]] | |||
[[Category: Zhu X]] | |||