Residue R113 Is Essential for PhoP Dimerization and Function: a Residue Buried in the Asymmetric PhoP Dimer Interface Determined in the PhoPN Three-Dimensional Crystal Structure
Author:
Affiliation:
1. Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607
2. Groupe de Cristallographie Biologique, CNRS-IPBS, 31077, Toulouse, France
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.185.1.262-273.2003
Reference47 articles.
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3. Birck C. Y. Chen F. M. Hulett and J.-P. Samama. 2003. The crystal structure of the regulatory domain in PhoP reveals a functional tandem association mediated by an asymmetric interface. J. Bacteriol. 185: 254-261.
4. Birck, C., L. Mourey, P. Gouet, B. Fabry, J. Schumacher, P. Rousseau, D. Kahn, and J. P. Samama. 1999. Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure Fold Des.7:1505-1515.
5. Birkey, S. M., W. Liu, X. Zhang, M. F. Duggan, and F. M. Hulett. 1998. Pho signal transduction network reveals direct transcriptional regulation of one two-component system by another two-component regulator: Bacillus subtilis PhoP directly regulates production of ResD. Mol. Microbiol.30:943-953.
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