This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Qamra, R. Articles by Mande, S. C. Search for Related Content PubMed PubMed Citation Articles by Qamra, R. Articles by Mande, S. C.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2004, p. 8105-8113, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8105-8113.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the 65-Kilodalton Heat Shock Protein, Chaperonin 60.2, of Mycobacterium tuberculosis

Rohini Qamra and Shekhar C. Mande^*

Centre for DNA Fingerprinting and Diagnostics, Nacharam, Hyderabad, India

Received 8 May 2004/ Accepted 4 August 2004

Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP-dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones. Chaperonin 60s are also known to be important stimulators of the immune system. Mycobacterium tuberculosis possesses a duplicate set of chaperonin 60s, both of which have been shown to be potent cytokine stimulators. The M. tuberculosis chaperonin 60s are present in the extracellular milieu at concentrations that are extremely low for the formation of an oligomer. Here we present the crystal structure of one of the chaperonin 60s of M. tuberculosis, also called Hsp65 or chaperonin 60.2, at 3.2-Å resolution. We were able to crystallize the protein in its dimeric state. The unusual dimerization of the protein leads to exposure of certain hydrophobic patches on the surface of the protein, and we hypothesize that this might have relevance in binding to immunogenic peptides, as it does in the eukaryotic homologs.

---

* Corresponding author. Mailing address: Centre for DNA Fingerprinting and Diagnostics, ECIL Road, Nacharam, Hyderabad 500076, India. Phone: 91-40-27171442. Fax: 91-40-27155610. E-mail: shekhar{at}cdfd.org.in.

---

Journal of Bacteriology, December 2004, p. 8105-8113, Vol. 186, No. 23
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.23.8105-8113.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Kumar, C. M. S., Khare, G., Srikanth, C. V., Tyagi, A. K., Sardesai, A. A., Mande, S. C. (2009). Facilitated Oligomerization of Mycobacterial GroEL: Evidence for Phosphorylation-Mediated Oligomerization. J. Bacteriol. 191: 6525-6538 [Abstract] [Full Text]  
• Hickey, T. B. M., Thorson, L. M., Speert, D. P., Daffe, M., Stokes, R. W. (2009). Mycobacterium tuberculosis Cpn60.2 and DnaK Are Located on the Bacterial Surface, Where Cpn60.2 Facilitates Efficient Bacterial Association with Macrophages. Infect. Immun. 77: 3389-3401 [Abstract] [Full Text]  
• Hu, Y., Henderson, B., Lund, P. A., Tormay, P., Ahmed, M. T., Gurcha, S. S., Besra, G. S., Coates, A. R. M. (2008). A Mycobacterium tuberculosis Mutant Lacking the groEL Homologue cpn60.1 Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection. Infect. Immun. 76: 1535-1546 [Abstract] [Full Text]  
• Rengarajan, J., Murphy, E., Park, A., Krone, C. L., Hett, E. C., Bloom, B. R., Glimcher, L. H., Rubin, E. J. (2008). Mycobacterium tuberculosis Rv2224c modulates innate immune responses. Proc. Natl. Acad. Sci. USA 105: 264-269 [Abstract] [Full Text]