| Literature DB >> 1334069 |
J Moore1, M Kantorow, D Vanderzwaag, K McKenney.
Abstract
The three-dimensional model of the Escherichia coli cyclic AMP (cAMP) receptor protein (CRP) shows that several amino acids are involved as chemical contacts for binding cAMP. We have constructed and characterized mutants at four of these positions, E72, R82, S83, and R123. The mutations were made in wild-type crp as well as a cAMP-independent crp, crp*. The activities of the mutant proteins were characterized in vivo for their ability to activate the lac operon. These results provide genetic evidence to support that E72 and R82 are essential and S83 and R123 are important in the activation of CRP by cAMP.Entities:
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Year: 1992 PMID: 1334069 PMCID: PMC207541 DOI: 10.1128/jb.174.24.8030-8035.1992
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490