Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium leprae

Shekhar C. Mande,  Vijay Mehra,  Barry R. Bloom,  Wim G. J. Hol (1)

Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resolution of 3.5 angstroms. The architecture of the Ml-cpn10 heptamer resembles a dome with an oculus in its roof. The inner surface of the dome is hydrophilic and highly charged. A flexible region, known to interact with cpn60, extends from the lower rim of the dome. With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.

S. C. Mande, Department of Biological Structure and Biomolecular Structure Center, University of Washington, Seattle, WA 98195, USA.
V. Mehra, Department of Microbiology and Immunology, University of Washington, Seattle, WA 98195, USA.
B. R. Bloom, Department of Microbiology and Immunology, University of Washington, Seattle, WA 98195, USA, and Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
W. G. J. Hol, Department of Biological Structure and Biomolecular Structure Center, and Howard Hughes Medical Institute, University of Washington, Box 357742, Seattle, WA 98195, USA. E-mail: hol@xray.bmsc.washington.edu
(1) To whom correspondence should be addressed.

This is the abstract of a paper which appeared in
Science Volume 271, Number 5246, Issue of 12 January 1996, pp. 203-207
©1996 by The American Association for the Advancement of Science.