4EHC
Crystal structure of the C-terminal domain of Rv0977 of Mycobacterium tuberculosis
Summary for 4EHC
| Entry DOI | 10.2210/pdb4ehc/pdb |
| Descriptor | PE-PGRS FAMILY PROTEIN, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | aspartic proteinase, hydrolase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 32271.06 |
| Authors | Barathy, D.V.,Suguna, K. (deposition date: 2012-04-02, release date: 2013-06-19, Last modification date: 2024-10-09) |
| Primary citation | Barathy, D.V.,Suguna, K. Crystal structure of a putative aspartic proteinase domain of the Mycobacterium tuberculosis cell surface antigen PE_PGRS16 FEBS Open Bio, 3:256-262, 2013 Cited by PubMed Abstract: We report the crystal structure of the first prokaryotic aspartic proteinase-like domain identified in the genome of Mycobacterium tuberculosis. A search in the genomes of Mycobacterium species showed that the C-terminal domains of some of the PE family proteins contain two classic DT/SG motifs of aspartic proteinases with a low overall sequence similarity to HIV proteinase. The three-dimensional structure of one of them, Rv0977 (PE_PGRS16) of M. tuberculosis revealed the characteristic pepsin-fold and catalytic site architecture. However, the active site was completely blocked by the N-terminal His-tag. Surprisingly, the enzyme was found to be inactive even after the removal of the N-terminal His-tag. A comparison of the structure with pepsins showed significant differences in the critical substrate binding residues and in the flap tyrosine conformation that could contribute to the lack of proteolytic activity of Rv0977. PubMed: 23923105DOI: 10.1016/j.fob.2013.05.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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