1qc7
From Proteopedia
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T. MARITIMA FLIG C-TERMINAL DOMAIN
Overview
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.
About this Structure
1QC7 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 00:33:55 2007
