View source for 9avi


==TolQ inner membrane protein from Acinetobacter baumannii==
<StructureSection load='9avi' size='340' side='right'caption='[[9avi]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9avi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9AVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9AVI 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]] 3.02&#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=9avi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9avi OCA], [https://pdbe.org/9avi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9avi RCSB], [https://www.ebi.ac.uk/pdbsum/9avi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9avi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5VAS0_ACIBA V5VAS0_ACIBA] Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.[HAMAP-Rule:MF_02202]
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== Publication Abstract from PubMed ==
Gram-negative bacteria harness the proton motive force (PMF) within their inner membrane (IM) to uphold the integrity of their cell envelope, an indispensable aspect for both division and survival. The IM TolQ-TolR complex is the essential part of the Tol-Pal system, serving as a conduit for PMF energy transfer to the outer membrane. Here we present cryo-EM reconstructions of Acinetobacter baumannii TolQ in apo and TolR- bound forms at atomic resolution. The apo TolQ configuration manifests as a symmetric pentameric pore, featuring a trans-membrane funnel leading towards a cytoplasmic chamber. In contrast, the TolQ-TolR complex assumes a proton non-permeable stance, characterized by the TolQ pentamer's flexure to accommodate the TolR dimer, where two protomers undergo a translation-based relationship. Our structure-guided analysis and simulations support the rotor-stator mechanism of action, wherein the rotation of the TolQ pentamer harmonizes with the TolR protomers' interplay. These findings broaden our mechanistic comprehension of molecular stator units empowering critical functions within the Gram-negative bacterial cell envelope. TEASER: Apo TolQ and TolQ-TolR structures depict structural rearrangements required for cell envelope organization in bacterial cell division.

Structural architecture of TolQ-TolR inner membrane protein complex from opportunistic pathogen Acinetobacter baumannii.,Karimullina E, Guo Y, Khan HM, Emde T, Quade B, Leo RD, Otwinowski Z, Tieleman Peter D, Borek D, Savchenko A bioRxiv [Preprint]. 2024 Jun 19:2024.06.19.599759. doi: , 10.1101/2024.06.19.599759. PMID:38948712<ref>PMID:38948712</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Borek D]]
[[Category: Otwinowski Z]]
[[Category: Quade B]]