2lp4
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2lp4 is ON HOLD Authors: dahlquist, F., Mo, G., Zhou, H., Kamamura, T. Description: Solution structure of P1-CheY/P2 complex in bacterial chemotaxi...) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of P1-CheY/P2 complex in bacterial chemotaxis== | |
| + | <StructureSection load='2lp4' size='340' side='right'caption='[[2lp4]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LP4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lp4 OCA], [https://pdbe.org/2lp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lp4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lp4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CHEA_ECOLI CHEA_ECOLI] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In the bacterial chemotaxis two-component signaling system, the histidine-containing phosphotransfer domain (the "P1" domain) of CheA receives a phosphoryl group from the catalytic domain (P4) of CheA and transfers it to the cognate response regulator (RR) CheY, which is docked by the P2 domain of CheA. Phosphorylated CheY then diffuses into the cytoplasm and interacts with the FliM moiety of the flagellar motors, thereby modulating the direction of flagellar rotation. Structures of various histidine phosphotransfer domains (HPt) complexed with their cognate RR domains have been reported. Unlike the Escherichia coli chemotaxis system, however, these systems lack the additional domains dedicated to binding to the response regulators, and the interaction of an HPt domain with an RR domain in the presence of such a domain has not been examined on a structural basis. In this study, we used modern nuclear magnetic resonance techniques to construct a model for the interaction of the E. coli CheA P1 domain (HPt) and CheY (RR) in the presence of the CheY-binding domain, P2. Our results indicate that the presence of P2 may lead to a slightly different relative orientation of the HPt and RR domains versus those seen in such complex structures previously reported. | ||
| - | + | Solution structure of a complex of the histidine autokinase CheA with its substrate CheY.,Mo G, Zhou H, Kawamura T, Dahlquist FW Biochemistry. 2012 May 8;51(18):3786-98. Epub 2012 Apr 26. PMID:22494339<ref>PMID:22494339</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lp4" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dahlquist F]] | ||
| + | [[Category: Kamamura T]] | ||
| + | [[Category: Mo G]] | ||
| + | [[Category: Zhou H]] | ||
Current revision
Solution structure of P1-CheY/P2 complex in bacterial chemotaxis
| |||||||||||
