大肠杆菌环磷酸腺苷受体蛋白突变体为激活过程中重要的配体接触提供了证据。
Escherichia coli cyclic AMP receptor protein mutants provide evidence for ligand contacts important in activation.
作者信息
Moore J, Kantorow M, Vanderzwaag D, McKenney K
机构信息
Center for Advanced Research in Biotechnology, Maryland Biotechnology Institute, Rockville.
出版信息
J Bacteriol. 1992 Dec;174(24):8030-5. doi: 10.1128/jb.174.24.8030-8035.1992.
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.
摘要
大肠杆菌环磷酸腺苷（cAMP）受体蛋白（CRP）的三维模型表明，有几个氨基酸作为结合cAMP的化学接触位点参与其中。我们在其中四个位置，即E72、R82、S83和R123构建并表征了突变体。这些突变在野生型crp以及一个不依赖cAMP的crp，即crp*中进行。突变蛋白的活性在体内通过其激活乳糖操纵子的能力进行表征。这些结果提供了遗传学证据，支持E72和R82是必需的，而S83和R123在cAMP激活CRP过程中很重要。
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