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The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

Nature volume 379, pages 37–45 (1996)Cite this article

Abstract

The GroES heptamer forms a dome, approximately 75 Å in diameter and 30 Å high, with an 8 Å orifice in the centre of its roof. The 'mobile loop' segment, previously identified as a GroEL binding determinant, is disordered in the crystal structure in six subunits; the single well-ordered copy extends from the bottom outer rim of the GroES dome, suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex.

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Author notes

  1. John F. Hunt & Arthur J. Weaver

    Present address: hkl Research Inc., 733 Seventh Avenue SWT, Rochester, Minnesota, 55902, USA

  2. Samuel J. Landry

    Present address: Department of Biochemistry, Tulane University School of Medicine, New Orleans, Louisiana, 70112, USA

  3. Lila Gierasch

    Present address: Department of Chemistry, University of Massachusetts, Amherst, Massachusetts, 01003, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Biochemistry, The University of Texas Southwestern Medical Center, Dallas, Texas, 75235, USA

    John F. Hunt, Arthur J. Weaver & Johann Deisenhofer

  2. Howard Hughes Medical Institute and Department of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75235, USA

    Samuel J. Landry & Lila Gierasch

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  1. John F. Hunt
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  2. Arthur J. Weaver
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  4. Lila Gierasch
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  5. Johann Deisenhofer
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Hunt, J., Weaver, A., Landry, S. et al. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 379, 37–45 (1996). https://doi.org/10.1038/379037a0

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