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 language | English (US) |
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Pages (from-to) | 170-177 |
Number of pages | 8 |
Journal | Nature Structural Biology |
Volume | 3 |
Issue number | 2 |
DOIs | |
State | Published - 1996 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics