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| Structure and catalytic mechanism of the E-coli chernotaxis phosphatase CheZ |
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| Author(s): Zhao R, Collins EJ, Bourret RB, Silversmith RE |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 9 Issue: 8 Pages: 570-575 Published: AUG 2002 |
| Times Cited: 67 References: 40 |
| Abstract: The protein CheZ, which has the last unknown structure in the Escherichia coli chemotaxis pathway, stimulates the dephosphorylation of the response regulator CheY by an unknown mechanism. Here we report the co-crystal structure of CheZ with CheY, Mg2+ and the phosphoryl analog, BeF3-. The predominant structural feature of the CheZ dimer is a long four-helix bundle composed of two helices from each monomer. The side chain of Gln 147 of CheZ inserts into the CheY active site and is essential to the dephosphorylation activity of CheZ. Gln 147 may orient a water molecule for nucleophilic attack, similar to the role of the conserved Gln residue in the RAS family of GTPases. Similarities between the CheY-CheZ and SpoOF-SpoOB structures suggest a general mode of interaction for modulation of response regulator phosphorylation chemistry. |
| Document Type: Article |
| Language: English |
| Reprint Address: Silversmith, RE (reprint author), Univ N Carolina, Dept Microbiol & Immunol, Chapel Hill, NC 27599 USA |
Addresses:
1. Univ N Carolina, Dept Microbiol & Immunol, Chapel Hill, NC 27599 USA |
| Publisher: NATURE AMERICA INC, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 USA |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: 580BK |
| ISSN: 1072-8368 |
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