7ri5: Difference between revisions
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==Structure of a BAM in MSP1E3D1 nanodiscs at 4 Angstrom resolution== | |||
<StructureSection load='7ri5' size='340' side='right'caption='[[7ri5]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ri5]] is a 5 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=7RI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RI5 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]] 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=7ri5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ri5 OCA], [https://pdbe.org/7ri5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ri5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ri5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ri5 ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Gram-negative bacteria, the biogenesis of beta-barrel outer membrane proteins is mediated by the beta-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely understood. Here, we report the structures of BAM in nanodiscs, prepared using polar lipids and native membranes, where we observe an outward-open state. Mutations in the barrel domain of BamA reveal that plasticity in BAM is essential, particularly along the lateral seam of the barrel domain, which is further supported by molecular dynamics simulations that show conformational dynamics in BAM are modulated by the accessory proteins. We also report the structure of BAM in complex with EspP, which reveals an early folding intermediate where EspP threads from the underside of BAM and incorporates into the barrel domain of BamA, supporting a hybrid-barrel budding mechanism in which the substrate is folded into the membrane sequentially rather than as a single unit. | |||
Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.,Wu R, Bakelar JW, Lundquist K, Zhang Z, Kuo KM, Ryoo D, Pang YT, Sun C, White T, Klose T, Jiang W, Gumbart JC, Noinaj N Nat Commun. 2021 Dec 8;12(1):7131. doi: 10.1038/s41467-021-27449-4. PMID:34880256<ref>PMID:34880256</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ri5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Bam complex 3D structures|Bam complex 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Noinaj N]] | |||
[[Category: Wu RR]] | |||
Latest revision as of 09:44, 21 November 2024
Structure of a BAM in MSP1E3D1 nanodiscs at 4 Angstrom resolutionStructure of a BAM in MSP1E3D1 nanodiscs at 4 Angstrom resolution
Structural highlights
FunctionBAMA_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.[1] [2] [3] [4] [5] Publication Abstract from PubMedIn Gram-negative bacteria, the biogenesis of beta-barrel outer membrane proteins is mediated by the beta-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely understood. Here, we report the structures of BAM in nanodiscs, prepared using polar lipids and native membranes, where we observe an outward-open state. Mutations in the barrel domain of BamA reveal that plasticity in BAM is essential, particularly along the lateral seam of the barrel domain, which is further supported by molecular dynamics simulations that show conformational dynamics in BAM are modulated by the accessory proteins. We also report the structure of BAM in complex with EspP, which reveals an early folding intermediate where EspP threads from the underside of BAM and incorporates into the barrel domain of BamA, supporting a hybrid-barrel budding mechanism in which the substrate is folded into the membrane sequentially rather than as a single unit. Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.,Wu R, Bakelar JW, Lundquist K, Zhang Z, Kuo KM, Ryoo D, Pang YT, Sun C, White T, Klose T, Jiang W, Gumbart JC, Noinaj N Nat Commun. 2021 Dec 8;12(1):7131. doi: 10.1038/s41467-021-27449-4. PMID:34880256[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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