4PMQ
Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with L-tartrate (orthorhombic crystal form)
Summary for 4PMQ
| Entry DOI | 10.2210/pdb4pmq/pdb |
| Descriptor | Tat-secreted protein Rv2525c, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | unknown function |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 22585.91 |
| Authors | Bellinzoni, M.,Haouz, A.,Shepard, W.,Alzari, P.M. (deposition date: 2014-05-22, release date: 2014-10-08, Last modification date: 2023-12-20) |
| Primary citation | Bellinzoni, M.,Haouz, A.,Miras, I.,Magnet, S.,Andre-Leroux, G.,Mukherjee, R.,Shepard, W.,Cole, S.T.,Alzari, P.M. Structural studies suggest a peptidoglycan hydrolase function for the Mycobacterium tuberculosis Tat-secreted protein Rv2525c. J.Struct.Biol., 188:156-164, 2014 Cited by PubMed Abstract: 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 β-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. PubMed: 25260828DOI: 10.1016/j.jsb.2014.09.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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