Document Detail


Sites of allosteric shift in the structure of the cyclic AMP receptor protein.
MedLine Citation:
PMID:  2988785     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have characterized crp mutations in E. coli that allow CRP to function without cAMP. crp* mutants carrying a deletion of the gene encoding adenylate cyclase (cya) show significant lac expression. Cyclic GMP, normally an ineffective activator of CRP+, can stimulate these mutant CRP*s to permit greater lac expression in vivo. Cyclic AMP binding to the amino-terminal domain of CRP+ induces an allosteric transition that changes the DNA-binding property of the carboxy domain. The CRP* phenotype is caused by substitution of amino acids with bulkier side chains in the D alpha-helix of the protein's carboxy domain, near the hinge connecting the two domains. These results are consistent with a model in which the mutant CRP*s assume, in part, a conformation normally evoked only by cAMP binding: one in which the relative orientation of the C, D, and F alpha-helices is altered. We define precisely the amino acids of these alpha-helices that interact to cause the allosteric shift.
Authors:
S Garges; S Adhya
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Cell     Volume:  41     ISSN:  0092-8674     ISO Abbreviation:  Cell     Publication Date:  1985 Jul 
Date Detail:
Created Date:  1985-07-31     Completed Date:  1985-07-31     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  745-51     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Base Sequence
Cyclic AMP / metabolism,  pharmacology*
Cyclic GMP / pharmacology
Escherichia coli / analysis
Genes
Mutation
Phenotype
Protein Conformation / drug effects
Receptors, Cyclic AMP* / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Receptors, Cyclic AMP; 60-92-4/Cyclic AMP; 7665-99-8/Cyclic GMP

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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