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TitleThe crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Journal, issue, pagesNature, Vol. 371, Issue 6498, Page 578-586, Year 1994
Publish dateOct 13, 1994
AuthorsK Braig / Z Otwinowski / R Hegde / D C Boisvert / A Joachimiak / A L Horwich / P B Sigler /
PubMed AbstractThe 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 ...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.
External linksNature / PubMed:7935790
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1grl:
THE CRYSTAL STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8 ANGSTROMS
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Source
  • escherichia coli (E. coli)
KeywordsCHAPERONIN

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