4pmq

Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with L-tartrate (orthorhombic crystal form)

spinqualitylabelsall models 4pmq, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pmq is a 1 chain structure with sequence from Mycobacterium tuberculosis CDC1551. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.61Å Ligands: GOL, TLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P95028_MYCTO Publication Abstract from PubMed Among the few proteins shown to be secreted by the Tat system in Mycobacterium tuberculosis, Rv2525c is of particular interest, since its gene is conserved in the minimal genome of Mycobacterium leprae. Previous evidence linked this protein to cell wall metabolism and sensitivity to beta-lactams. We describe here the crystal structure of Rv2525c that shows a TIM barrel-like fold characteristic of glycoside hydrolases of the GH25 family, which includes prokaryotic and phage-encoded peptidoglycan hydrolases. Structural comparison with other members of this family combined with substrate docking suggest that, although the 'neighbouring group' catalytic mechanism proposed for this family still appears as the most plausible, the identity of residues involved in catalysis in GH25 hydrolases might need to be revised. Structural studies suggest a peptidoglycan hydrolase function for the Mycobacterium tuberculosis Tat-secreted protein Rv2525c.,Bellinzoni M, Haouz A, Miras I, Magnet S, Andre-Leroux G, Mukherjee R, Shepard W, Cole ST, Alzari PM J Struct Biol. 2014 Sep 24. pii: S1047-8477(14)00189-0. doi:, 10.1016/j.jsb.2014.09.003. PMID:25260828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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