GHKL, an emergent ATPase/kinase superfamily

Trends Biochem Sci. 2000 Jan;25(1):24-8. doi: 10.1016/s0968-0004(99)01503-0.

Abstract

An interesting recent development is the recognition of a novel ATP-binding superfamily that includes diverse protein families such as DNA topoisomerase II, molecular chaperones Hsp90, DNA-mismatch-repair enzymes MutL and histidine kinases. The most singular unifying feature of this superfamily is the unconventional Bergerat ATP-binding fold. The far-reaching significance of this commonality is still in the process of being explored.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphatases*
  • Adenosine Triphosphate / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Catalytic Domain
  • DNA Topoisomerases, Type II / chemistry
  • DNA Topoisomerases, Type II / metabolism*
  • Escherichia coli Proteins*
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / metabolism*
  • Histidine Kinase
  • Hydrolysis
  • Molecular Sequence Data
  • MutL Proteins
  • Protein Folding
  • Protein Kinases / chemistry
  • Protein Kinases / metabolism*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • HSP90 Heat-Shock Proteins
  • MutL protein, E coli
  • Adenosine Triphosphate
  • Protein Kinases
  • Histidine Kinase
  • Adenosine Triphosphatases
  • MutL Proteins
  • DNA Topoisomerases, Type II