2I5D

Crystal Structure of Human Inosine Triphosphate Pyrophosphatase

2I5D の概要

• エントリーDOI: 10.2210/pdb2i5d/pdb
• 関連するPDBエントリー: 2CAR
• 分子名称: inosine triphosphate pyrophosphohydrolase (2 entities in total)
• 機能のキーワード: monomeric protein, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q9BY32
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21750.90

構造登録者

Porta, J.C.,Kozmin, S.G.,Pavlov, Y.I.,Borgstahl, G.E.O. (登録日: 2006-08-24, 公開日: 2006-09-05, 最終更新日: 2023-08-30)

主引用文献

Porta, J.,Kolar, C.,Kozmin, S.G.,Pavlov, Y.I.,Borgstahl, G.E.O.
Structure of the orthorhombic form of human inosine triphosphate pyrophosphatase.
Acta Crystallogr.,Sect.F, 62:1076-1081, 2006

PubMed Abstract: The structure of human inosine triphosphate pyrophosphohydrolase (ITPA) has been determined using diffraction data to 1.6 A resolution. ITPA contributes to the accurate replication of DNA by cleansing cellular dNTP pools of mutagenic nucleotide purine analogs such as dITP or dXTP. A similar high-resolution unpublished structure has been deposited in the Protein Data Bank from a monoclinic and pseudo-merohedrally twinned crystal. Here, cocrystallization of ITPA with a molar ratio of XTP appears to have improved the crystals by eliminating twinning and resulted in an orthorhombic space group. However, there was no evidence for bound XTP in the structure. Comparison with substrate-bound NTPase from a thermophilic organism predicts the movement of residues within helix alpha1, the loop before alpha6 and helix alpha7 to cap off the active site when substrate is bound.

PubMed: 17077483
DOI: 10.1107/S1744309106041790

実験手法

X-RAY DIFFRACTION (1.63 Å)