1IUU

P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 9.4

1IUU の概要

• エントリーDOI: 10.2210/pdb1iuu/pdb
• 分子名称: P-HYDROXYBENZOATE HYDROXYLASE, FLAVIN-ADENINE DINUCLEOTIDE, 4-AMINOBENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45305.23

構造登録者

Gatti, D.L.,Entsch, B.,Ballou, D.P.,Ludwig, M.L. (登録日: 1995-11-22, 公開日: 1996-04-03, 最終更新日: 2024-02-07)

主引用文献

Gatti, D.L.,Entsch, B.,Ballou, D.P.,Ludwig, M.L.
pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.
Biochemistry, 35:567-578, 1996

PubMed Abstract: Deprotonation of p-hydroxybenzoate to the phenolate and reprotonation of the hydroxylated dienone intermediate to form the product are essential steps in the reaction catalyzed by p-hydroxybenzoate hydroxylase (PHBH). The mechanism by which protons are transferred in these reactions is not obvious, because the substrate bound in the active site is isolated from solvent. Structure analyses of wild-type and mutant PHBH, with bound p-hydroxybenzoate or p-aminobenzoate, reveal a chain of proton donors and acceptors (the hydroxyl groups of Tyr201 and Tyr385, and two water molecules) that can connect the substrate 4-OH to His72, a surface residue. This chain could provide a pathway for proton transfer to and from the substrate. Using various combinations of pH and substrates, we show that in crystalline PHBH ionizable groups in the chain may rotate and change hydrogen-bond orientation. Molecular dynamics simulations have been used to predict the preferred orientation of hydrogen bonds in the chain as a function of the ionization states of substrate and His72. The calculations suggest that changes in the ionization state of the substrate could be associated with changes in orientation of the hydrogen bonds in the chain. Transfer of water between the chain of proton donors and the solvent also appears to be an essential part of the mechanism that provides reversible transfer of protons during the hydroxylation reaction.

PubMed: 8555229
DOI: 10.1021/bi951344i

実験手法

X-RAY DIFFRACTION (2 Å)