8bnz

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Current revision (11:56, 23 October 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8bnz]] 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=8BNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BNZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[8bnz]] 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=8BNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BNZ FirstGlance]. <br>
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</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=8bnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bnz OCA], [https://pdbe.org/8bnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bnz RCSB], [https://www.ebi.ac.uk/pdbsum/8bnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bnz ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bnz OCA], [https://pdbe.org/8bnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bnz RCSB], [https://www.ebi.ac.uk/pdbsum/8bnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bnz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://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>
[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8bnz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Current revision

BAM-EspP complex structure with BamA-G431C/EspP-N1293C mutations in nanodisc

PDB ID 8bnz

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