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 journalArticlepeer-review

16 Scopus citations

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 1 1999

ASJC Scopus subject areas

  • Structural Biology

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