2OLC
Crystal structure of 5-methylthioribose kinase in complex with ADP-2Ho
Summary for 2OLC
| Entry DOI | 10.2210/pdb2olc/pdb |
| Descriptor | Methylthioribose kinase, HOLMIUM ATOM, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ... (5 entities in total) |
| Functional Keywords | kinase adp-2ho complex, transferase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 92408.94 |
| Authors | Ku, S.Y.,Smith, G.D.,Howell, P.L. (deposition date: 2007-01-18, release date: 2007-05-22, Last modification date: 2023-12-27) |
| Primary citation | Ku, S.Y.,Smith, G.D.,Howell, P.L. ADP-2Ho as a phasing tool for nucleotide-containing proteins. Acta Crystallogr.,Sect.D, 63:493-499, 2007 Cited by PubMed Abstract: Trivalent holmium ions were shown to isomorphously replace magnesium ions to form an ADP-2Ho complex in the nucleotide-binding domain of Bacillus subtilis 5-methylthioribose (MTR) kinase. This nucleotide-holmium complex provided sufficient phasing power to allow SAD and SIRAS phasing of this previously unknown structure using the L(III) absorption edge of holmium. The structure of ADP-2Ho reveals that the two Ho ions are approximately 4 A apart and are likely to share their ligands: the phosphoryl O atoms of ADP and a water molecule. The structure determination of MTR kinase using data collected using Cu Kalpha X-radiation was also attempted. Although the heavy-atom substructure determination was successful, interpretation of the map was more challenging. The isomorphous substitution of holmium for magnesium in the MTR kinase-nucleotide complex suggests that this could be a useful phasing tool for other metal-dependent nucleotide-containing proteins. PubMed: 17372354DOI: 10.1107/S0907444907006592 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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