The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

Nat Struct Biol. 1996 Feb;3(2):170-7. doi: 10.1038/nsb0296-170.


GroEL is a bacterial chaperonin of 14 identical subunits required to help fold newly synthesized proteins. The crystal structure of GroEL with ATP gamma S bound to each subunit shows that ATP binds to a novel pocket, whose primary sequence is highly conserved among chaperonins. Interaction of Mg2+ and ATP involves phosphate oxygens of the alpha-, beta- and gamma-phosphates, which is unique for known structures of nucleotide-binding proteins. Although bound ATP induces modest conformational shifts in the equatorial domain, the stereochemistry that functionally coordinates GroEL's affinity for nucleotides, polypeptide, and GroES remains uncertain.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives*
  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Binding Sites
  • Chaperonin 60 / chemistry*
  • Chaperonin 60 / metabolism
  • Crystallography, X-Ray
  • Magnesium / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation


  • Chaperonin 60
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • Magnesium