1JON

GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345

Summary for 1JON

• Entry DOI: 10.2210/pdb1jon/pdb
• Descriptor: GROEL, HSP60 CLASS (2 entities in total)
• Functional Keywords: chaperone, cell division, atp-binding, phosphorylation
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6F5
• Total number of polymer chains: 1
• Total formula weight: 16642.24

Authors

Buckle, A.M.,Fersht, A.R. (deposition date: 1996-05-30, release date: 1997-03-12, Last modification date: 2024-05-22)

Primary citation

Zahn, R.,Buckle, A.M.,Perrett, S.,Johnson, C.M.,Corrales, F.J.,Golbik, R.,Fersht, A.R.
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
Proc.Natl.Acad.Sci.USA, 93:15024-15029, 1996

PubMed Abstract: The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.

PubMed: 8986757
DOI: 10.1073/pnas.93.26.15024

Experimental method

X-RAY DIFFRACTION (2.5 Å)