The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein

Shaoning Yu, Rodrigo A. Maillard, Alexey V. Gribenko, J. Ching Lee

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Background: Residue 138 situates in the hinge region connecting the DNA- and cAMP-binding domains of CRP. Results: A correlation was established among N-capping propensities and cooperativity of cAMP binding and affinity for lac-DNA. Conclusion: Our results provide a quantitative characterization of the N-capping properties of residue 138 in the allosteric activation event. Significance: The results provide the thermodynamic basis to the structural model of allostery.

Original languageEnglish (US)
Pages (from-to)39402-39411
Number of pages10
JournalJournal of Biological Chemistry
Volume287
Issue number47
DOIs
StatePublished - Nov 16 2012

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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