4iga

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<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=4iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iga RCSB], [http://www.ebi.ac.uk/pdbsum/4iga PDBsum]</span></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=4iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iga RCSB], [http://www.ebi.ac.uk/pdbsum/4iga PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/CHEY_THEMA CHEY_THEMA]] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation (By similarity). [[http://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA]] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 02:45, 25 December 2014

The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM

4iga, resolution 1.73Å

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