Multiple Conformations of the FliG C-Terminal Domain Provide Insight into Flagellar Motor Switching
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摘要Bacterial flagellar switching between counterclockwise and clockwise directions is mediated by the coupling of the chemotactic system and the motor switch complex. The conformational changes of FliG are closely associated with this switching mechanism. We present two crystal structures of FliG(MG) from Helicobacter pylori, each showing distinct domain orientations from previously solved structures. A 180 degrees rotation of the charged ridge-containing C-terminal subdomain FliG(C alpha 1-6) that is prompted by the rotational freedom of Met245 psi and Phe246 phi at the MFXF motif was revealed. Studies on the swarming and swimming behavior of Escherichia coli mutants further identified the importance of the 245MFXF248 motif and a highly conserved residue, Asn216, in motor switching. Additionally, multiple conformations of FliG(C alpha 1-6) were demonstrated by intramolecular cysteine crosslinking. The conformational flexibility of FliGc leads us to propose a model that accounts for the symmetrical torque generation process and for the dynamics of the motor.
著者Lam KH, Ip WS, Lam YW, Chan SO, Ling TKW, Au SWN
期刊名稱Structure
出版年份2012
月份2
日期8
卷號20
期次2
出版社Elsevier (Cell Press)
頁次315 - 325
國際標準期刊號0969-2126
語言英式英語
Web of Science 學科類別Biochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY; Biophysics; BIOPHYSICS; Cell Biology; CELL BIOLOGY

上次更新時間 2020-13-10 於 00:46