Rebuttal: Beryllofluoride binding mimics phosphorylation of aspartate in response regulators

Journal of Bacteriology

Volumn 187, Issue 24, 2005, Pages 8231-

  Varughese, Kottayil I ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN; BERYLLIUM; BERYLLOFLUORIDE; DNA; FLUORIDE; SPOOF PROTEIN; UNCLASSIFIED DRUG;

BACTERIAL SPORE; BINDING AFFINITY; CRYSTAL STRUCTURE; DNA BINDING; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; METAL BINDING; NONHUMAN; NOTE; PHENOTYPE; PRIORITY JOURNAL; SPOROGENESIS;

ASPARTIC ACID; BACTERIAL PROTEINS; BERYLLIUM; CRYSTALLOGRAPHY, X-RAY; FLUORIDES; MOLECULAR MIMICRY; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SECOND MESSENGER SYSTEMS;

BACTERIA (MICROORGANISMS);

EID: 28844499013     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.24.8231.2005     Document Type: Note

References (5)

1. --activated Spo0F reveals the conformational switch in a phosphorelay system. J. Mol. Biol. 331:245-254.
2. Tzeng, Y. L., and J. A. Hoch. 1997. Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis. J. Mol. Biol. 272:200-212.
3. Varughese, K. I. 2005. Conformational changes of Spo0F along the phosphotransfer pathway. J. Bacteriol. 187:8221-8227.
4. Wemmer, D. E., and D. Kern. 2005. Beryllofluoride binding mimics phosphorylation of aspartate in response regulators. J. Bacteriol. 187:8229-8230.
5. Zapf, J., U. Sen, Madhusudan, J. A. Hoch, and K. I. Varughese. 2000. A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Struct. Folding Design 8:851-862.