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Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.

Wang J, Boisvert DC
J Mol Biol 327 843-55 (2003)
Cited: 100 times
EuropePMC logo PMID: 12654267

Abstract

Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with high affinity in the absence of ATP and with low affinity in its presence. We report the crystal structure of (GroEL-KMgATP)(14) refined to 2.0 A resolution in which the ATP triphosphate moiety is directly coordinated by both K(+) and Mg(2+). Upon the binding of KMgATP, we observe previously unnoticed domain rotations and a 102 degrees rotation of the apical domain surface helix I. Two major consequences are a large lateral displacement of, and a dramatic reduction of hydrophobicity in, the apical domain surface. These results provide a basis for the nucleotide-dependent regulation of protein substrate binding and suggest a mechanism for GroEL-assisted protein folding by forced unfolding.

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Articles - 1kp8 mentioned but not cited (41)

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Related citations provided by authors (4)

  1. The 2.4 A Crystal Structure of the Bacterial Chaperonin GroEL Complexed with ATP Gamma S. Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB Nat. Struct. Biol. 3 170-177 (1996)
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  4. The Crystal Structure of the Asymmetric GroEL-GroES-(ADP)7 Chaperonin Complex. Xu Z, Horwich AL, Sigler PB Nature 388 741-750 (1997)

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