Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS

Journal of Bacteriology

Volumn 191, Issue 18, 2009, Pages 5842-5844

  Hao, Shufeng ^a   Hamel, Damon ^a   Zhou, Hongjun ^a   Dahlquist, Frederick W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; CHEA KINASE; CHEZ PROTEIN; DIMER; UNCLASSIFIED DRUG;

ARTICLE; CELL POLARITY; CHEMOTAXIS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; BINDING SITES; CHEMOTAXIS; DIMERIZATION; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, MOLECULAR; NITROGEN ISOTOPES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTONS; SIGNAL TRANSDUCTION;

EID: 69949111846     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00323-09     Document Type: Article

References (12)

1. Cantwell, B. J., R. R. Draheim, R. B. Weart, C. Nguyen, R. C. Stewart, and M. D. Manson. 2003. CheZ phosphatase localizes to chemoreceptor patches via CheA-short. J. Bacteriol. 185:2354-2361.
2. Glushka, J., M. Lee, S. Coffin, and D. Cowburn. 1989. 15N chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin. J. Am. Chem. Soc. 111:7716-7722.
3. Kay, L. E., D. A. Torchia, and A. Bax. 1989. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28:8972-8979.
4. Maddock, J. R., and L. Shapiro. 1993. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259:1717-1723. (Pubitemid 23114656)
5. O'Connor, C., and P. Matsumura. 2004. The accessibility of Cys-120 in CheAS is important for the binding of CheZ and enhancement of CheZ phosphatase activity. Biochemistry 43:6909-6916. (Pubitemid 38720509)
6. Sattler, M., J. Schleucher, and C. Griesinger. 1999. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34:93-158.
7. Smith, R. A., and J. S. Parkinson. 1980. Overlapping genes at the cheA locus of Escherichia coli. Proc. Natl. Acad. Sci. USA 77:5370-5374.
8. Sourjik, V., and H. C. Berg. 2000. Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 37:740-751.
9. Vaknin, A., and H. C. Berg. 2004. Single-cell FRET imaging of phosphatase activity in the Escherichia coli chemotaxis system. Proc. Natl. Acad. Sci. USA 101:17072-17077.
10. S/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. Mol. Microbiol. 19:695-703.
11. Wishart, D. S., and B. D. Sykes. 1994. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical- shift data. J. Biomol. NMR 4:171-180.
12. Wishart, D. S., B. D. Sykes, and F. M. Richards. 1992. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.