Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from klebsiella pneumoniae

Shih Chi Luo; Yuan Chao Lou; Mahalingam Rajasekaran; Yi Wei Chang; Chwan Deng Hsiao; Chinpan Chen

doi:10.1074/jbc.M113.481978

Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from klebsiella pneumoniae

Shih Chi Luo, Yuan Chao Lou, Mahalingam Rajasekaran, Yi Wei Chang, Chwan Deng Hsiao, Chinpan Chen

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state. Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions. Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation. Significance: This work provides novel data revealing how a connector protein protects an activated response regulator.

Original language	English (US)
Pages (from-to)	25551-25561
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	35
DOIs	https://doi.org/10.1074/jbc.M113.481978
State	Published - Aug 30 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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abstract = "Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state. Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions. Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation. Significance: This work provides novel data revealing how a connector protein protects an activated response regulator.",

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AU - Luo, Shih Chi

AU - Lou, Yuan Chao

AU - Rajasekaran, Mahalingam

AU - Chang, Yi Wei

AU - Hsiao, Chwan Deng

AU - Chen, Chinpan

PY - 2013/8/30

Y1 - 2013/8/30

N2 - Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state. Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions. Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation. Significance: This work provides novel data revealing how a connector protein protects an activated response regulator.

AB - Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state. Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions. Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation. Significance: This work provides novel data revealing how a connector protein protects an activated response regulator.

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Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from klebsiella pneumoniae

Abstract

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