1KP8: Structural Basis For Groel-assisted Protein Folding From The Crystal Structure Of (groel-kmgatp)14 At 2.0 A Resolution

Citation:
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.
PDB ID: 1KP8Download
MMDB ID: 71214
PDB Deposition Date: 2001/12/30
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1KP8: tetradecameric; determined by author and by software (PISA)
Molecular Components in 1KP8
Label Count Molecule
Proteins (14 molecules)
14
Groel Protein(Gene symbol: groL)
Molecule annotation
Chemicals (66 molecules)
1
22
2
14
3
16
4
14
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.