3OEI
Crystal structure of Mycobacterium tuberculosis RelJK (Rv3357-Rv3358-RelBE3)
Summary for 3OEI
Entry DOI | 10.2210/pdb3oei/pdb |
Descriptor | RelJ (Antitoxin Rv3357), RelK (Toxin Rv3358), CITRATE ANION, ... (5 entities in total) |
Functional Keywords | toxin-antitoxin systems, protein-protein complex, tuberculosis structural genomics consortium, toxin, protein binding, tb structural genomics consortium, tbsgc |
Biological source | Mycobacterium tuberculosis More |
Total number of polymer chains | 16 |
Total formula weight | 179262.03 |
Authors | Miallau, L.,Cascio, D.,Eisenberg, D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2010-08-12, release date: 2011-03-16, Last modification date: 2023-09-20) |
Primary citation | Miallau, L.,Jain, P.,Arbing, M.A.,Cascio, D.,Phan, T.,Ahn, C.J.,Chan, S.,Chernishof, I.,Maxson, M.,Chiang, J.,Jacobs Jr., W.R.,Eisenberg, D.S. Comparative proteomics identifies the cell-associated lethality of M. tuberculosis RelBE-like toxin-antitoxin complexes. Structure, 21:627-637, 2013 Cited by PubMed Abstract: The Mycobacterium tuberculosis (Mtb) genome encodes approximately 90 toxin-antitoxin protein complexes, including three RelBE family members, which are believed to play a major role in bacterial fitness and pathogenicity. We have determined the crystal structures of Mtb RelBE-2 and RelBE-3, and the structures reveal homologous heterotetramers. Our structures suggest RelE-2, and by extension the closely related RelE-1, use a different catalytic mechanism than RelE-3, because our analysis of the RelE-2 structure predicts additional amino acid residues that are likely to be functionally significant and are missing from analogous positions in the RelE-3 structure. Toxicity assays corroborate our structural findings; overexpression of RelE-3, whose active site is more similar to Escherichia coli YoeB, has limited consequences on bacterial growth, whereas RelE-1 and RelE-2 overexpression results in acute toxicity. Moreover, RelE-2 overexpression results in an elongated cell phenotype in Mycobacterium smegmatis and protects M. tuberculosis against antibiotics, suggesting a different functional role for RelE-2. PubMed: 23523424DOI: 10.1016/j.str.2013.02.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.145 Å) |
Structure validation
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