1KP8

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution

Replaces:  1DER

Summary for 1KP8

• Entry DOI: 10.2210/pdb1kp8/pdb
• Related: 1J4Z 1KPO
• Descriptor: groEL protein, SULFATE ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: chaperonin, groel, assisted protein folding, chaperone
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6F5
• Total number of polymer chains: 14
• Total formula weight: 810229.99

Authors

Wang, J. (deposition date: 2001-12-30, release date: 2003-03-25, Last modification date: 2024-02-14)

Primary citation

Wang, J.,Boisvert, D.C.
Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution
J.Mol.Biol., 327:843-855, 2003

PubMed 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.

PubMed: 12654267
DOI: 10.1016/S0022-2836(03)00184-0

Experimental method

X-RAY DIFFRACTION (2 Å)