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Science 12 January 1996:
Vol. 271. no. 5246, pp. 203 - 207
DOI: 10.1126/science.271.5246.203
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Reports
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{at}xray.bmsc.washington.edu
(1) To whom correspondence should be addressed.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Mycobacterium tuberculosis Chaperonin 10 Heptamers Self-Associate through Their Biologically Active Loops.
- M. M. Roberts, A. R. Coker, G. Fossati, P. Mascagni, A. R. M. Coates, and S. P. Wood (2003)
J. Bacteriol.
185, 4172-4185
| Abstract »
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- Mycobacterium tuberculosis Chaperonin 10 Is Secreted in the Macrophage Phagosome: Is Secretion Due to Dissociation and Adoption of a Partially Helical Structure at the Membrane?.
- G. Fossati, G. Izzo, E. Rizzi, E. Gancia, D. Modena, M. L. Moras, N. Niccolai, E. Giannozzi, O. Spiga, L. Bono, et al. (2003)
J. Bacteriol.
185, 4256-4267
| Abstract »
| Full Text »
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- Recombinant GroES in combination with CpG oligodeoxynucleotides protects mice against Mycobacterium avium infection.
- L. FATTORINI, R. CRETI, R. NISINI, R. PIETROBONO, Y. FAN, A. STRINGARO, G. ARANCIA, O. SERLUPI-CRESCENZI, E. IONA, and G. OREFICI (2002)
J. Med. Microbiol.
51, 1071-1079
| Abstract »
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- Metal ions modulate the plastic nature of Mycobacterium tuberculosis chaperonin-10.
- B. Taneja and S. C. Mande (2001)
Protein Eng. Des. Sel.
14, 391-395
| Abstract »
| Full Text »
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- Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.
- M. Fändrich, M. A. Tito, M. R. Leroux, A. A. Rostom, F. U. Hartl, C. M. Dobson, and C. V. Robinson (2000)
PNAS
| Abstract »
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- Differential T-Cell Recognition of Native and Recombinant Mycobacterium tuberculosis GroES.
- I. Rosenkrands, K. Weldingh, P. Ravn, L. Brandt, P. Hojrup, P. B. Rasmussen, A. R. Coates, M. Singh, P. Mascagni, and P. Andersen (1999)
Infect. Immun.
67, 5552-5558
| Abstract »
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- Conserved structural features and sequence patterns in the GroES fold family.
- B. Taneja and S. C. Mande (1999)
Protein Eng. Des. Sel.
12, 815-818
| Abstract »
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- Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.
- M. S. Goldberg, J. Zhang, S. Sondek, C. R. Matthews, R. O. Fox, and A. L. Horwich (1997)
PNAS
94, 1080-1085
| Abstract »
| Full Text »
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- Catalysis of protein folding by symmetric chaperone complexes.
- H. Sparrer, K. Rutkat, and J. Buchner (1997)
PNAS
94, 1096-1100
| Abstract »
| Full Text »
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- The effect of macromolecular crowding on chaperonin-mediated protein folding.
- J. Martin and F.-U. Hartl (1997)
PNAS
94, 1107-1112
| Abstract »
| Full Text »
| PDF »
- Symmetry, stability, and dynamics of multidomain and multicomponent protein systems.
- T. L. Blundell and N. Srinivasan (1996)
PNAS
93, 14243-14248
| Abstract »
| Full Text »
| PDF »
- GroEL Locked in a Closed Conformation by an Interdomain Cross-link Can Bind ATP and Polypeptide but Cannot Process Further Reaction Steps.
- N. Murai, Y. Makino, and M. Yoshida (1996)
J. Biol. Chem.
271, 28229-28234
| Abstract »
| Full Text »
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- Interactions of GroEL/GroES with a Heterodimeric Intermediate during alpha 2beta 2 Assembly of Mitochondrial Branched-chain alpha -Ketoacid Dehydrogenase. cis CAPPING OF THE NATIVE-LIKE 86-kDa INTERMEDIATE BY GroES.
- J.-L. Song, R. M. Wynn, and D. T. Chuang (2000)
J. Biol. Chem.
275, 22305-22312
| Abstract »
| Full Text »
| PDF »
- Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.
- M. Fandrich, M. A. Tito, M. R. Leroux, A. A. Rostom, F. U. Hartl, C. M. Dobson, and C. V. Robinson (2000)
PNAS
97, 14151-14155
| Abstract »
| Full Text »
| PDF »
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