3UID
Crystal Structure of Protein Ms6760 from Mycobacterium smegmatis
Summary for 3UID
| Entry DOI | 10.2210/pdb3uid/pdb |
| Descriptor | Putative uncharacterized protein (2 entities in total) |
| Functional Keywords | uncharacterized protein, srpbcc superfamily, beta sandwich, unknown function, structural genomics, tb structural genomics consortium, tbsgc |
| Biological source | Mycobacterium smegmatis |
| Total number of polymer chains | 2 |
| Total formula weight | 37134.78 |
| Authors | Bajaj, R.A.,Miallau, L.,Cascio, D.,Arbing, M.,Eisenberg, D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2011-11-04, release date: 2011-11-23, Last modification date: 2023-09-13) |
| Primary citation | Bajaj, R.A.,Arbing, M.A.,Shin, A.,Cascio, D.,Miallau, L. Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response. Acta Crystallogr F Struct Biol Commun, 72:863-869, 2016 Cited by PubMed Abstract: The structure of Msmeg_6760, a protein of unknown function, has been determined. Biochemical and bioinformatics analyses determined that Msmeg_6760 interacts with a protein encoded in the same operon, Msmeg_6762, and predicted that the operon is a toxin-antitoxin (TA) system. Structural comparison of Msmeg_6760 with proteins of known function suggests that Msmeg_6760 binds a hydrophobic ligand in a buried cavity lined by large hydrophobic residues. Access to this cavity could be controlled by a gate-latch mechanism. The function of the Msmeg_6760 toxin is unknown, but structure-based predictions revealed that Msmeg_6760 and Msmeg_6762 are homologous to Rv2034 and Rv2035, a predicted novel TA system involved in Mycobacterium tuberculosis latency during macrophage infection. The Msmeg_6760 toxin fold has not been previously described for bacterial toxins and its unique structural features suggest that toxin activation is likely to be mediated by a novel mechanism. PubMed: 27917833DOI: 10.1107/S2053230X16017957 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.571 Å) |
Structure validation
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