1JKN

Solution Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus angustifolius Complexed with ATP

1JKN の概要

• エントリーDOI: 10.2210/pdb1jkn/pdb
• 関連するPDBエントリー: 1F3Y
• NMR情報: BMRB: 5054
• 分子名称: diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: alpha-beta-alpha sandwich, enzyme-substrate complex, hydrolase
• 由来する生物種: Lupinus angustifolius (narrow-leaved blue lupine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19341.35

構造登録者

Fletcher, J.I.,Swarbrick, J.D.,Maksel, D.,Gayler, K.R.,Gooley, P.R. (登録日: 2001-07-12, 公開日: 2002-02-27, 最終更新日: 2024-05-22)

主引用文献

Fletcher, J.I.,Swarbrick, J.D.,Maksel, D.,Gayler, K.R.,Gooley, P.R.
The structure of Ap(4)A hydrolase complexed with ATP-MgF(x) reveals the basis of substrate binding.
Structure, 10:205-213, 2002

PubMed Abstract: Ap(4)A hydrolases are Nudix enzymes that regulate intracellular dinucleoside polyphosphate concentrations, implicating them in a range of biological events, including heat shock and metabolic stress. We have demonstrated that ATP x MgF(x) can be used to mimic substrates in the binding site of Ap(4)A hydrolase from Lupinus angustifolius and that, unlike previous substrate analogs, it is in slow exchange with the enzyme. The three-dimensional structure of the enzyme complexed with ATP x MgF(x) was solved and shows significant conformational changes. The substrate binding site of L. angustifolius Ap(4)A hydrolase differs markedly from the two previously published Nudix enzymes, ADP-ribose pyrophosphatase and MutT, despite their common fold and the conservation of active site residues. The majority of residues involved in substrate binding are conserved in asymmetrical Ap(4)A hydrolases from pathogenic bacteria, but are absent in their human counterparts, suggesting that it might be possible to generate compounds that target bacterial, but not human, Ap(4)A hydrolases.

PubMed: 11839306
DOI: 10.1016/S0969-2126(02)00696-2

実験手法

SOLUTION NMR