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

doi:10.1074/jbc.M112.404806

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 journal › Article › peer-review

10 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 language	English (US)
Pages (from-to)	39402-39411
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	287
Issue number	47
DOIs	https://doi.org/10.1074/jbc.M112.404806
State	Published - Nov 16 2012
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

author = "Shaoning Yu and Maillard, {Rodrigo A.} and Gribenko, {Alexey V.} and Lee, {J. Ching}",

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T1 - The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein

AU - Yu, Shaoning

AU - Maillard, Rodrigo A.

AU - Gribenko, Alexey V.

AU - Lee, J. Ching

PY - 2012/11/16

Y1 - 2012/11/16

N2 - 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.

AB - 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.

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

Abstract

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