1OT3

Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine

1OT3 の概要

• エントリーDOI: 10.2210/pdb1ot3/pdb
• 分子名称: Deoxyribonucleoside Kinase, SULFATE ION, THYMIDINE, ... (4 entities in total)
• 機能のキーワード: protein-deoxynucleoside complex, transferase
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 235820.43

構造登録者

Mikkelsen, N.E.,Johansson, K.,Karlsson, A.,Knecht, W.,Andersen, G.,Piskur, J.,Munch-Petersen, B.,Eklund, H. (登録日: 2003-03-21, 公開日: 2003-05-27, 最終更新日: 2023-10-25)

主引用文献

Mikkelsen, N.E.,Johansson, K.,Karlsson, A.,Knecht, W.,Andersen, G.,Piskur, J.,Munch-Petersen, B.,Eklund, H.
Structural Basis for Feedback Inhibition of the Deoxyribonucleoside Salvage Pathway: Studies of the Drosophila Deoxyribonucleoside Kinase.
Biochemistry, 42:5706-5712, 2003

PubMed Abstract: 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.

PubMed: 12741827
DOI: 10.1021/bi0340043

実験手法

X-RAY DIFFRACTION (2.5 Å)