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1ot3

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{{STRUCTURE_1ot3| PDB=1ot3 | SCENE= }}
{{STRUCTURE_1ot3| PDB=1ot3 | SCENE= }}
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'''Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine'''
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===Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine===
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==Overview==
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Deoxyribonucleoside kinases are feedback inhibited by the final products of the salvage pathway, the deoxyribonucleoside triphosphates. In the present study, the mechanism of feedback inhibition is presented based on the crystal structure of a complex between the fruit fly deoxyribonucleoside kinase and its feedback inhibitor deoxythymidine triphosphate. The inhibitor was found to be bound as a bisubstrate inhibitor with its nucleoside part in the nucleoside binding site and with its phosphate groups partially occupying the phosphate donor site. The overall structure of the enzyme--inhibitor complex is very similar to the enzyme--substrate complexes with deoxythymidine and deoxycytidine, except for a conformational change within a region otherwise directly involved in catalysis. This conformational change involves a magnesium ion, which is coordinated in the inhibitor complex to the phosphates and to the primary base, Glu52, that normally is positioned close to the 5'-OH of the substrate deoxyribose.
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{{ABSTRACT_PUBMED_12741827}}
==About this Structure==
==About this Structure==
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[[Category: Piskur, J.]]
[[Category: Piskur, J.]]
[[Category: Protein-deoxynucleoside complex]]
[[Category: Protein-deoxynucleoside complex]]
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Revision as of 09:47, 28 July 2008

Image:1ot3.png

Template:STRUCTURE 1ot3

Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine

Template:ABSTRACT PUBMED 12741827

About this Structure

1OT3 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Structural basis for feedback inhibition of the deoxyribonucleoside salvage pathway: studies of the Drosophila deoxyribonucleoside kinase., Mikkelsen NE, Johansson K, Karlsson A, Knecht W, Andersen G, Piskur J, Munch-Petersen B, Eklund H, Biochemistry. 2003 May 20;42(19):5706-12. PMID:12741827

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