2olc: Difference between revisions

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==Overview==
==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.
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.L.]]
[[Category: Howell, P L.]]
[[Category: Ku, S.Y.]]
[[Category: Ku, S Y.]]
[[Category: Smith, G.D.]]
[[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]]


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Revision as of 19:19, 21 February 2008

File:2olc.jpg


2olc, resolution 2.000Å

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Crystal structure of 5-methylthioribose kinase in complex with ADP-2Ho

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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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