1vlz

<table><tr><td colspan='2'>[[1vlz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLZ FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlz OCA], [http://pdbe.org/1vlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vlz RCSB], [http://www.ebi.ac.uk/pdbsum/1vlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlz ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CHEY_ECOLI CHEY_ECOLI]] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.<ref>PMID:20346719</ref>

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== Publication Abstract from PubMed ==

Position 87 of the chemotaxis regulatory protein CheY is a highly conserved threonine/serine residue in the response regulator superfamily. A threonine 87 to isoleucine mutant in CheY, identified by its in vivo non-chemotactic phenotype, was also found to be phosphorylatable in vitro. These properties indicate that this mutant does not undergo activation upon phosphorylation. The x-ray crystallographic structure of the threonine to isoleucine CheY mutant has been solved and refined at 2.1-A resolution, to an R factor of 15.6%. Comparison with the wild-type, Mg(2+)-free CheY structure shows that the active site structure is retained, but there are significant localized differences in the backbone conformation distal from the substitution. The presence of the isoleucine side chain also restricts the rotational conformation of another conserved residue in the molecule, tyrosine at position 106. These results provide further evidence for a signaling surface remote from the phosphorylation site of the CheY molecule and implicate threonine 87 and other residues in the post-phosphorylation signaling events.

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY.,Ganguli S, Wang H, Matsumura P, Volz K J Biol Chem. 1995 Jul 21;270(29):17386-93. PMID:7615544<ref>PMID:7615544</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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[[Category: Bacillus coli migula 1895]]

[[Category: Ganguli, S]]

[[Category: Matsumura, P]]

[[Category: Volz, K]]

[[Category: Wang, H]]

[[Category: Two-component system]]