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Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS.
Hao, Shufeng; Hamel, Damon; Zhou, Hongjun; Dahlquist, Frederick W.
Affiliation
  • Hao S; Department of Chemistry and Biochemistry, University of California-Santa Barbara, Santa Barbara, CA 93106, USA.
J Bacteriol ; 191(18): 5842-4, 2009 Sep.
Article in En | MEDLINE | ID: mdl-19502407
ABSTRACT
CheA-short interacts with CheZ to localize CheZ to cell poles. The fifth helical region (residues 112 to 133) from the phosphotransfer domain of CheA interacts with CheZ and becomes ordered and helical, although it lacks a stable fold in the CheA fragment comprising residues 98 to 150 alone. One CheA molecule binds to one CheZ dimer.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Chemotaxis / Escherichia coli / Membrane Proteins Language: En Journal: J Bacteriol Year: 2009 Document type: Article Affiliation country: United States
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Chemotaxis / Escherichia coli / Membrane Proteins Language: En Journal: J Bacteriol Year: 2009 Document type: Article Affiliation country: United States