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

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

D C Boisvert  1 , J Wang, Z Otwinowski, A L Horwich, P B Sigler
Affiliations

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

D C Boisvert et al. Nat Struct Biol. 1996 Feb.

Abstract

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.

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  • GroE structures galore.
    Lorimer GH, Todd MJ. Lorimer GH, et al. Nat Struct Biol. 1996 Feb;3(2):116-21. doi: 10.1038/nsb0296-116. Nat Struct Biol. 1996. PMID: 8564534 No abstract available.

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