1qc7

<table><tr><td colspan='2'>[[1qc7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QC7 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FLIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc7 OCA], [http://pdbe.org/1qc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qc7 RCSB], [http://www.ebi.ac.uk/pdbsum/1qc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qc7 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) 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 ==

Many motile species of bacteria are propelled by flagella, which are rigid helical filaments turned by rotary motors in the cell membrane. The motors are powered by the transmembrane gradient of protons or sodium ions. Although bacterial flagella contain many proteins, only three-MotA, MotB and FliG-participate closely in torque generation. MotA and MotB are ion-conducting membrane proteins that form the stator of the motor. FliG is a component of the rotor, present in about 25 copies per flagellum. It is composed of an amino-terminal domain that functions in flagellar assembly and a carboxy-terminal domain (FliG-C) that functions specifically in motor rotation. Here we report the crystal structure of FliG-C from the hyperthermophilic eubacterium Thermotoga maritima. Charged residues that are important for function, and which interact with the stator protein MotA, cluster along a prominent ridge on FliG-C. On the basis of the disposition of these residues, we present a hypothesis for the orientation of FliG-C domains in the flagellar motor, and propose a structural model for the part of the rotor that interacts with the stator.

Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor.,Lloyd SA, Whitby FG, Blair DF, Hill CP Nature. 1999 Jul 29;400(6743):472-5. PMID:10440379<ref>PMID:10440379</ref>

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

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== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Blair, D]]

[[Category: Hill, C P]]

[[Category: Lloyd, S A]]

[[Category: Whitby, F G]]

[[Category: Flagellar motor switch protein]]

[[Category: Structural protein]]