2Z9I
Crystal structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form
Summary for 2Z9I
| Entry DOI | 10.2210/pdb2z9i/pdb |
| Related | 1ky9 1l1j 1sot |
| Descriptor | PROBABLE SERINE PROTEASE PEPD, SVEQV, GATV, ... (4 entities in total) |
| Functional Keywords | serine protease, htra, hydrolase |
| Biological source | Mycobacterium tuberculosis More |
| Total number of polymer chains | 9 |
| Total formula weight | 99827.71 |
| Authors | Palaninathan, S.K.,Mohamedmohaideen, N.N.,Sacchettini, J.C. (deposition date: 2007-09-20, release date: 2008-06-10, Last modification date: 2024-10-30) |
| Primary citation | Mohamedmohaideen, N.N.,Palaninathan, S.K.,Morin, P.M.,Williams, B.J.,Braunstein, M.,Tichy, S.E.,Locker, J.,Russell, D.H.,Jacobs, W.R.,Sacchettini, J.C. Structure and function of the virulence-associated high-temperature requirement A of Mycobacterium tuberculosis Biochemistry, 47:6092-6102, 2008 Cited by PubMed Abstract: The high-temperature requirement A (HtrA) family of serine proteases has been shown to play an important role in the environmental and cellular stress damage control system in Escherichia coli. Mycobacterium tuberculosis ( Mtb) has three putative HtrA-like proteases, HtrA1, HtrA2, and HtrA3. The deletion of htrA2 gives attenuated virulence in a mouse model of TB. Biochemical analysis reveals that HtrA2 can function both as a protease and as a chaperone. The three-dimensional structure of HtrA2 determined at 2.0 A resolution shows that the protease domains form the central core of the trimer and the PDZ domains extend to the periphery. Unlike E. coli DegS and DegP, the protease is naturally active due to the formation of the serine protease-like catalytic triad and its uniquely designed oxyanion hole. Both protease and PDZ binding pockets of each HtrA2 molecule are occupied by autoproteolytic peptide products and reveal clues for a novel autoregulatory mechanism that might have significant importance in HtrA-associated virulence of Mtb. PubMed: 18479146DOI: 10.1021/bi701929m PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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