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2olc
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(New page: 200px<br /><applet load="2olc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2olc, resolution 2.000Å" /> '''Crystal structure o...)
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Revision as of 11:05, 21 November 2007
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Crystal structure of 5-methylthioribose kinase in complex with ADP-2Ho
Overview
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.
About this Structure
2OLC is a Single protein structure of sequence from Bacillus subtilis with HO, CPS and ADP as ligands. Active as S-methyl-5-thioribose kinase, with EC number 2.7.1.100 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 13:13:12 2007
