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The crystal structure of YycH involved in the regulation of the essential YycFG two‐component system in Bacillus subtilis reveals a novel tertiary structure
Author(s) -
Szurmant Hendrik,
Zhao Haiyan,
Mohan Michael A.,
Hoch James A.,
Varughese Kottayil I.
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.052064406
Subject(s) - bacillus subtilis , component (thermodynamics) , chemistry , signal transduction , domain (mathematical analysis) , protein tertiary structure , biophysics , biology , physics , biochemistry , genetics , bacteria , mathematics , mathematical analysis , thermodynamics
The Bacillus subtilis YycFG two‐component signal transduction system is essential for cell viability, and the YycH protein is part of the regulatory circuit that controls its activity. The crystal structure of YycH was solved by two‐wavelength selenium anomalous dispersion data, and was refined using 2.3 Å data to an R ‐factor of 25.2%. The molecule is made up of three domains, and has a novel three‐dimensional structure. The N‐terminal domain features a calcium binding site and the central domain contains two conserved loop regions.