Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB

Masato Kato, Takeshi Mizuno, Toshiyuki Shimizu, Toshio Hakoshima

Research output: Contribution to journalArticle

124 Citations (Scopus)

Abstract

The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined at 2.06 Å resolution. The domain consists of six α helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes.

Original languageEnglish (US)
Pages (from-to)717-723
Number of pages7
JournalCell
Volume88
Issue number5
DOIs
StatePublished - Mar 7 1997

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Histidine
Crystal structure
Eukaryota
Phosphotransferases
Sensors
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. / Kato, Masato; Mizuno, Takeshi; Shimizu, Toshiyuki; Hakoshima, Toshio.

In: Cell, Vol. 88, No. 5, 07.03.1997, p. 717-723.

Research output: Contribution to journalArticle

Kato, Masato ; Mizuno, Takeshi ; Shimizu, Toshiyuki ; Hakoshima, Toshio. / Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB. In: Cell. 1997 ; Vol. 88, No. 5. pp. 717-723.
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