Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 Å resolution

Masato Kato, Takeshi Mizuno, Toshiyuki Shimizu, Toshio Hakoshima

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The crystal structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to 1.57 Å resolution, using the coordinates of the earlier 2.06 Å structure as a starting model. The final model contained 956 protein atoms, one zinc ion and 156 water molecules, with an R factor of 19.0%. The high-resolution electron-density maps clearly revealed additional solvent molecules and seven discrete rotamers in the protein side chains. One residue, Met755, was fully buried but was able to occupy the space in the hydrophobic core by means of the two-state conformation of its side chain. One water molecule was buried in the protein core and contributed to the rigidity of the HPt domain, cooperating in the coordination of the zinc ion.

Original languageEnglish (US)
Pages (from-to)1842-1849
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number11
DOIs
StatePublished - Nov 1999

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histidine
Escherichia
Histidine
Escherichia coli
Phosphotransferases
proteins
Molecules
Zinc
sensors
Sensors
zinc
Ions
molecules
Proteins
Water
R Factors
rigidity
Rigidity
water
Carrier concentration

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 Å resolution. / Kato, Masato; Mizuno, Takeshi; Shimizu, Toshiyuki; Hakoshima, Toshio.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 11, 11.1999, p. 1842-1849.

Research output: Contribution to journalArticle

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