View source for 7ri4


==Structure of a BAM/EspP(beta9-12) hybrid-barrel intermediate==
<StructureSection load='7ri4' size='340' side='right'caption='[[7ri4]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ri4]] 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=7RI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RI4 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]] 3.4&#8491;</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=7ri4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ri4 OCA], [https://pdbe.org/7ri4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ri4 RCSB], [https://www.ebi.ac.uk/pdbsum/7ri4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ri4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESPP_ECOLX ESPP_ECOLX] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ri4" 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]]