The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli

BMC Struct Biol. 2004 Aug 11:4:9. doi: 10.1186/1472-6807-4-9.

Abstract

Background: ChaB is a putative regulator of ChaA, a Na+/H+ antiporter that also has Ca+/H+ activity in E. coli. ChaB contains a conserved 60-residue region of unknown function found in other bacteria, archaeabacteria and a series of baculoviral proteins. As part of a structural genomics project, the structure of ChaB was elucidated by NMR spectroscopy.

Results: The structure of ChaB is composed of 3 alpha-helices and a small sheet that pack tightly to form a fold that is found in the cyclin-box family of proteins.

Conclusion: ChaB is distinguished from its putative DNA binding sequence homologues by a highly charged flexible loop region that has weak affinity to Mg2+ and Ca2+ divalent metal ions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cations / metabolism
  • Cloning, Molecular / methods
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / physiology
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Peptides / physiology
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary / physiology
  • Sodium-Calcium Exchanger / physiology

Substances

  • Cations
  • ChaB protein, E coli
  • Escherichia coli Proteins
  • Peptides
  • Sodium-Calcium Exchanger