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

Cell. 1997 Mar 7;88(5):717-23. doi: 10.1016/s0092-8674(00)81914-5.


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 A resolution. The domain consists of six alpha 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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography
  • Drug Design
  • Escherichia coli Proteins*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Metals / metabolism
  • Methyl-Accepting Chemotaxis Proteins
  • Molecular Sequence Data
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Protein Kinases*
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid


  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Metals
  • Methyl-Accepting Chemotaxis Proteins
  • Phosphoproteins
  • Protein Kinases
  • arcB protein, E coli