View source for 9biz


==Crystal structure of the periplasmic domain of IgaA from Klebsiella pneumoniae==
<StructureSection load='9biz' size='340' side='right'caption='[[9biz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9biz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BIZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=9biz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9biz OCA], [https://pdbe.org/9biz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9biz RCSB], [https://www.ebi.ac.uk/pdbsum/9biz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9biz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0AA35H6S5_KLEPN A0AA35H6S5_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Rcs pathway is repressed by the inner membrane protein IgaA under non-stressed conditions. This repression is hypothesized to be relieved by the binding of the outer membrane-anchored RcsF to IgaA. However, the precise mechanism by which RcsF binding triggers the signaling remains unclear. Here, we present the 1.8 A resolution crystal structure capturing the interaction between IgaA and RcsF. Our comparative structural analysis, examining both the bound and unbound states of the periplasmic domain of IgaA (IgaAp), highlights rotational flexibility within IgaAp. Conversely, the conformation of RcsF remains unchanged upon binding. Our in vivo and in vitro studies do not support the model of a stable complex involving RcsF, IgaAp, and RcsDp. Instead, we demonstrate that the elements beyond IgaAp play a role in the interaction between IgaA and RcsD. These findings collectively allow us to propose a potential mechanism for the signaling across the inner membrane through IgaA.

Molecular insights into the initiation step of the Rcs signaling pathway.,Watanabe N, Savchenko A Structure. 2024 Jun 25:S0969-2126(24)00221-1. doi: 10.1016/j.str.2024.06.003. PMID:38964336<ref>PMID:38964336</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9biz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Savchenko A]]
[[Category: Watanabe N]]