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Title
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The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.
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Authors
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D.C.Boisvert,
J.Wang,
Z.Otwinowski,
A.L.Horwich,
P.B.Sigler.
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Ref.
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Nat Struct Biol, 1996,
3,
170-177.
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PubMed id
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Abstract
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GroEL is a bacterial chaperonin of 14 identical subunits required to help fold
newly synthesized proteins. The crystal structure of GroEL with ATP gamma S
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 alpha-, beta- and gamma-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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