2olc
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Trivalent holmium ions were shown to isomorphously replace magnesium ions | + | 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== | ==About this Structure== | ||
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[[Category: S-methyl-5-thioribose kinase]] | [[Category: S-methyl-5-thioribose kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Howell, P | + | [[Category: Howell, P L.]] |
| - | [[Category: Ku, S | + | [[Category: Ku, S Y.]] |
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CPS]] | [[Category: CPS]] | ||
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[[Category: kinase adp-2ho complex]] | [[Category: kinase adp-2ho complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:45 2008'' |
Revision as of 16:19, 21 February 2008
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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 , and 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
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