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

John F. Hunt, Arthur J. Weaver, Samuel J. Landry, Lila Gierasch, Johann Deisenhofer

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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.

Original languageEnglish (US)
Pages (from-to)37-45
Number of pages9
JournalNature
Volume379
Issue number6560
DOIs
StatePublished - Jan 4 1996

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Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L., & Deisenhofer, J. (1996). The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature, 379(6560), 37-45. https://doi.org/10.1038/379037a0