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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

Academic Article
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Overview

authors

  • Szurmant, Hendrik
  • Zhao, H. Y.
  • Mohan, M. A.
  • Hoch, James
  • Varughese, K. I.

publication date

  • April 2006

journal

  • Protein Science  Journal

abstract

  • 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 A 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.

subject areas

  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Conserved Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression Regulation, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Signal Transduction
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Research

keywords

  • YycF
  • YycG
  • YycH
  • calcium binding
  • histidine kinase
  • response regulator
  • signal transduction
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Identity

PubMed Central ID

  • PMC2242482

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1110/ps.052064406

PubMed ID

  • 16600972
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Additional Document Info

start page

  • 929

end page

  • 934

volume

  • 15

issue

  • 4

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