1GRL

THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS

Summary for 1GRL

• Entry DOI: 10.2210/pdb1grl/pdb
• Descriptor: GROEL (HSP60 CLASS) (1 entity in total)
• Functional Keywords: chaperonin
• Biological source: Escherichia coli
• Total number of polymer chains: 7
• Total formula weight: 400942.72

Authors

Braig, K.,Otwinowski, Z.,Hegde, R.,Boisvert, D.C.,Joachimiak, A.,Horwich, A.L.,Sigler, P.B. (deposition date: 1995-03-07, release date: 1995-10-15, Last modification date: 2024-02-07)

Primary citation

Braig, K.,Otwinowski, Z.,Hegde, R.,Boisvert, D.C.,Joachimiak, A.,Horwich, A.L.,Sigler, P.B.
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Nature, 371:578-586, 1994

PubMed Abstract: The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.

PubMed: 7935790
DOI: 10.1038/371578a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)