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

David C. Boisvert, Jimin Wang, Zbyszek Otwinowski, Arthur L. Horwich, Paul B. Sigler

Research output: Contribution to journalArticle

237 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)170-177
Number of pages8
JournalNature Structural Biology
Volume3
Issue number2
DOIs
StatePublished - Jan 1 1996

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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