2BI0
RV0216, A conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdogfold
Summary for 2BI0
| Entry DOI | 10.2210/pdb2bi0/pdb |
| Descriptor | HYPOTHETICAL PROTEIN RV0216, CHLORIDE ION (3 entities in total) |
| Functional Keywords | hypothetical protein, conserved hypothetical, rv0216, mycobacterium tuberculosis, hotdog-fold, structural proteomics in europe, spine, structural genomics |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 35975.60 |
| Authors | Castell, A.,Johansson, P.,Unge, T.,Jones, T.A.,Backbro, K. (deposition date: 2005-01-20, release date: 2005-04-25, Last modification date: 2024-10-16) |
| Primary citation | Castell, A.,Johansson, P.,Unge, T.,Jones, T.A.,Backbro, K. Rv0216, a Conserved Hypothetical Protein from Mycobacterium Tuberculosis that is Essential for Bacterial Survival During Infection, Has a Double Hotdog Fold Protein Sci., 14:1850-, 2005 Cited by PubMed Abstract: The Mycobacterium tuberculosis genome contains about 4000 genes, of which approximately a third code for proteins of unknown function or are classified as conserved hypothetical proteins. We have determined the three-dimensional structure of one of these, the rv0216 gene product, which has been shown to be essential for M. tuberculosis growth in vivo. The structure exhibits the greatest similarity to bacterial and eukaryotic hydratases that catalyse the R-specific hydration of 2-enoyl coenzyme A. However, only part of the catalytic machinery is conserved in Rv0216 and it showed no activity for the substrate crotonyl-CoA. The structure of Rv0216 allows us to assign new functional annotations to a family of seven other M. tuberculosis proteins, a number if which are essential for bacterial survival during infection and growth. PubMed: 15987908DOI: 10.1110/PS.051442305 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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