2olc
Crystal structure of 5-methylthioribose kinase in complex with ADP-2HoCrystal structure of 5-methylthioribose kinase in complex with ADP-2Ho
Structural highlights
FunctionMTNK_BACSU Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTrivalent 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. ADP-2Ho as a phasing tool for nucleotide-containing proteins.,Ku SY, Smith GD, Howell PL Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):493-9. Epub 2007, Mar 16. PMID:17372354[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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