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The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS

Nature Structural Biology volume 3, pages 170–177 (1996)Cite this article

Abstract

GroEL is a bacterial chaperonin of 14 identical subunits required to help fold newly synthesized proteins. The crystal structure of GroEL with ATPγS 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 α-, β- and γ-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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Authors and Affiliations

  1. Department of Genetics, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, Connecticut, 06510, USA

    David C. Boisvert & Arthur L. Norwich

  2. Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, Connecticut, 06510, USA

    Jimin Wang, Zbyszek Otwinowski & Paul B. Sigler

  3. The Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, Connecticut, 06510, USA

    Arthur L. Norwich & Paul B. Sigler

  4. Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas, 75235, USA

    Zbyszek Otwinowski

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Boisvert, D., Wang, J., Otwinowski, Z. et al. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nat Struct Mol Biol 3, 170–177 (1996). https://doi.org/10.1038/nsb0296-170

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