4ehc

Crystal structure of the C-terminal domain of Rv0977 of Mycobacterium tuberculosis

spinqualitylabelsall models 4ehc, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ehc is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: EDO, MSE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG16_MYCTU Publication Abstract from PubMed 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. Crystal structure of a putative aspartic proteinase domain of the Mycobacterium tuberculosis cell surface antigen PE_PGRS16.,Barathy DV, Suguna K FEBS Open Bio. 2013 Jun 8;3:256-62. doi: 10.1016/j.fob.2013.05.004. Print 2013. PMID:23923105 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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