Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY

Masato Kato, Toshiyuki Shimizu, Takeshi Mizuno, Toshio Hakoshima

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 Å resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.

Original languageEnglish (US)
Pages (from-to)1257-1263
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number7
DOIs
StatePublished - Jul 1999

Fingerprint

histidine
regulators
Chemotaxis
Histidine
proteins
sensors
Sensors
Molecules
Proteins
molecules
Rigid structures
R Factors
rigid structures
Sulfates
sulfates
Ions
Atoms
Crystals
cells
crystals

ASJC Scopus subject areas

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

Cite this

Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY. / Kato, Masato; Shimizu, Toshiyuki; Mizuno, Takeshi; Hakoshima, Toshio.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 7, 07.1999, p. 1257-1263.

Research output: Contribution to journalArticle

@article{8534926214654f60bdb2833d2144e32a,
title = "Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY",
abstract = "The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3{\%} at 2.68 {\AA} resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.",
author = "Masato Kato and Toshiyuki Shimizu and Takeshi Mizuno and Toshio Hakoshima",
year = "1999",
month = "7",
doi = "10.1107/S0907444999005053",
language = "English (US)",
volume = "55",
pages = "1257--1263",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "7",

}

TY - JOUR

T1 - Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY

AU - Kato, Masato

AU - Shimizu, Toshiyuki

AU - Mizuno, Takeshi

AU - Hakoshima, Toshio

PY - 1999/7

Y1 - 1999/7

N2 - The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 Å resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.

AB - The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 Å resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.

UR - http://www.scopus.com/inward/record.url?scp=0033166624&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033166624&partnerID=8YFLogxK

U2 - 10.1107/S0907444999005053

DO - 10.1107/S0907444999005053

M3 - Article

C2 - 10393292

AN - SCOPUS:0033166624

VL - 55

SP - 1257

EP - 1263

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 7

ER -