View source for 7tt3


==BamABCDE bound to substrate EspP class 5==
<StructureSection load='7tt3' size='340' side='right'caption='[[7tt3]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7tt3]] 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=7TT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TT3 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]] 4.3&#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=7tt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tt3 OCA], [https://pdbe.org/7tt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tt3 RCSB], [https://www.ebi.ac.uk/pdbsum/7tt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tt3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BAME_ECOLI BAME_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD.<ref>PMID:17404237</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> <ref>PMID:21207987</ref> <ref>PMID:21586578</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transmembrane beta barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the beta barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. Here, we used single-particle cryo-EM to visualize the folding dynamics of a model beta barrel protein (EspP) by BAM. We found that BAM binds the highly conserved "beta signal" motif of EspP to correctly orient beta strands in the OM during folding. We also found that the folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated beta sheets are attached to the essential BAM subunit, BamA. The structures show an unprecedented deflection of the membrane surrounding the EspP intermediates and suggest that beta sheets progressively fold toward BamA to form a beta barrel. Along with in vivo experiments that tracked beta barrel folding while the OM tension was modified, our results support a model in which BAM harnesses OM elasticity to accelerate beta barrel folding.

Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.,Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, Bernstein HD Cell. 2022 Mar 31;185(7):1143-1156.e13. doi: 10.1016/j.cell.2022.02.016. Epub , 2022 Mar 15. PMID:35294859<ref>PMID:35294859</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tt3" 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: Bernstein HD]]
[[Category: Dowdy T]]
[[Category: Doyle MT]]
[[Category: Hinshaw JE]]
[[Category: Jimah JR]]
[[Category: Larion M]]
[[Category: Ohlemacher SI]]