3QVA

Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase

3QVA の概要

• エントリーDOI: 10.2210/pdb3qva/pdb
• 分子名称: Transthyretin-like protein, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: transthyretin-related protein, 5-hydroxyisourate hydrolase, hydrolase
• 由来する生物種: Klebsiella pneumoniae subsp. pneumoniae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49957.18

構造登録者

French, J.B.,Ealick, S.E. (登録日: 2011-02-25, 公開日: 2011-08-24, 最終更新日: 2024-02-21)

主引用文献

French, J.B.,Ealick, S.E.
Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae.
Acta Crystallogr.,Sect.D, 67:671-677, 2011

PubMed Abstract: The stereospecific oxidative degradation of uric acid to (S)-allantoin has recently been demonstrated to proceed via two unstable intermediates and requires three separate enzymatic reactions. The second step of this reaction, the conversion of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline, is catalyzed by HIU hydrolase (HIUH). The high-resolution crystal structure of HIUH from the opportunistic pathogen Klebsiella pneumoniae (KpHIUH) has been determined. KpHIUH is a homotetrameric protein that, based on sequence and structural similarity, belongs to the transthyretin-related protein family. In addition, the steady-state kinetic parameters for this enzyme and four active-site mutants have been measured. These data provide valuable insight into the functional roles of the active-site residues. Based upon the structural and kinetic data, a mechanism is proposed for the KpHIUH-catalyzed reaction.

PubMed: 21795808
DOI: 10.1107/S090744491101746X

実験手法

X-RAY DIFFRACTION (1.755 Å)