1KTG

Crystal Structure of a C. elegans Ap4A Hydrolase Binary Complex

1KTG の概要

• エントリーDOI: 10.2210/pdb1ktg/pdb
• 関連するPDBエントリー: 1KT9
• 分子名称: Diadenosine Tetraphosphate Hydrolase, PHOSPHATE ION, HYDROXIDE ION, ... (6 entities in total)
• 機能のキーワード: nudix, amp, magnesium cluster, hydrolase
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32616.19

構造登録者

Bailey, S.,Sedelnikova, S.E.,Blackburn, G.M.,Abdelghany, H.M.,Baker, P.J.,McLennan, A.G.,Rafferty, J.B. (登録日: 2002-01-16, 公開日: 2002-05-08, 最終更新日: 2023-08-16)

主引用文献

Bailey, S.,Sedelnikova, S.E.,Blackburn, G.M.,Abdelghany, H.M.,Baker, P.J.,McLennan, A.G.,Rafferty, J.B.
The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms
Structure, 10:589-600, 2002

PubMed Abstract: The crystal structure of C. elegans Ap(4)A hydrolase has been determined for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively. Ap(4)A hydrolase has a key role in regulating the intracellular Ap(4)A levels and hence potentially the cellular response to metabolic stress and/or differentiation and apoptosis via the Ap(3)A/Ap(4)A ratio. The structures reveal that the enzyme has the mixed alpha/beta fold of the Nudix family and also show how the enzyme binds and locates its substrate with respect to the catalytic machinery of the Nudix motif. These results suggest how the enzyme can catalyze the hydrolysis of a range of related dinucleoside tetraphosphate, but not triphosphate, compounds through precise orientation of key elements of the substrate.

PubMed: 11937063
DOI: 10.1016/S0969-2126(02)00746-3

実験手法

X-RAY DIFFRACTION (1.8 Å)