These comprise homologues of GroEL and GroES chaperonins. Crystal structure of the chaperonin-10 was recently elucidated in our laboratory. The structure shows many interesting features, including providing an evidence for its divalent metal binding properties, which might explain some of the clinical symptoms arising due to secretion of the protein. Work on the GroEL homologues has also been initiated.
 

Recent publications:

1. Structure of Mycobacterium Tuberculosis chaperonin-10 at 3.5 A resoluiton.
   B. Taneja and S. C. Mande
   Acta Crystallogr (2002) D58, 260-266.
2. Crystal structure of Mycobacterium tuberculosis chaperonin-10 reveals a partially stable conformation of its mobile loop.
   B. Taneja and S. C. Mande
   Curr. Sci. (2001) 81, 87- 91.
3. Metal ions modulate the plastic nature of M. tuberculosis chaperonin-10.
   B. Taneja and S. C. Mande
   Prot Eng. (2001) 14, 391- 395.
   (See also the cover of Protein Engineering).
4. Conserved sequence patterns and structural features of the GroES- fold proteins.
   B. Taneja and S. C. Mande
   Prot. Eng. (1999) 12, 815- 818.