3DBO
Crystal structure of a member of the VapBC family of toxin-antitoxin systems, VapBC-5, from Mycobacterium tuberculosis
Summary for 3DBO
| Entry DOI | 10.2210/pdb3dbo/pdb |
| Descriptor | Uncharacterized protein, SODIUM ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | toxin antitoxin complex, vapbc, mycobacterium tuberculosis, structural genomics, psi-2, protein structure initiative, integrated center for structure and function innovation, isfi, tb structural genomics consortium, tbsgc, toxin-antitoxin complex, toxin/antitoxin |
| Biological source | Mycobacterium tuberculosis More |
| Total number of polymer chains | 2 |
| Total formula weight | 26648.12 |
| Authors | Miallau, L.,Cascio, D.,Eisenberg, D.,Integrated Center for Structure and Function Innovation (ISFI),TB Structural Genomics Consortium (TBSGC) (deposition date: 2008-06-02, release date: 2008-07-15, Last modification date: 2024-02-21) |
| Primary citation | Miallau, L.,Faller, M.,Chiang, J.,Arbing, M.,Guo, F.,Cascio, D.,Eisenberg, D. Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems: VapBC-5 FROM MYCOBACTERIUM TUBERCULOSIS. J.Biol.Chem., 284:276-283, 2009 Cited by PubMed Abstract: In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis. Here we report the crystal structure and activity of a member of the VapBC family of complexes from M. tuberculosis. The toxin VapC-5 is a compact, 150 residues, two domain alpha/beta protein. Bent around the toxin is the VapB-5 antitoxin, a 33-residue alpha-helix. Assays suggest that the toxin is an Mg-enabled endoribonuclease, inhibited by the antitoxin. The lack of DNase activity is consistent with earlier suggestions that the complex represses its own operon. Furthermore, analysis of the interactions in the binding of the antitoxin to the toxin suggest that exquisite control is required to protect the bacteria cell from toxic VapC-5. PubMed: 18952600DOI: 10.1074/jbc.M805061200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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