9RB2

Crystal Structure of glxR

9RB2 の概要

• エントリーDOI: 10.2210/pdb9rb2/pdb
• Group deposition: the group title you wish to show (1)
• 分子名称: Probable oxidoreductase (2 entities in total)
• 機能のキーワード: glxr, tartronate semialdehyde reductase, glyoxylate, transferase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 131962.44

構造登録者

Parkhill, S.,little, O.,Wang, M.,Askenasy, I.,Brear, P.,Cai, W.,Welch, M. (登録日: 2025-05-21, 公開日: 2025-12-24, 最終更新日: 2026-01-14)

主引用文献

Parkhill, S.L.,Little, O.,Askenasy, I.,Labrini, E.,Wang, M.,Brear, P.D.,Cai, W.,Deingruber, T.,Yang, T.,Spring, D.R.,Welch, M.
An allantoin-inducible glyoxylate utilization pathway in Pseudomonas aeruginosa.
Microbiology (Reading, Engl.), 171:-, 2025

PubMed Abstract: Fluorescent pseudomonads catabolize purines via uric acid and allantoin, a pathway whose end-product is glyoxylate. In this work, we show that in strain PAO1, the ORFs PA1498-PA1502 encode a pathway that converts the resulting glyoxylate into pyruvate. The expression of this cluster of ORFs was stimulated in the presence of allantoin, and mutants containing transposon insertions in the cluster were unable to grow on allantoin as a sole carbon source. The likely operonic structure of the cluster is elucidated. We also show that the purified proteins encoded by PA1502 and PA1500 have glyoxylate carboligase (Gcl) and tartronate semialdehyde (TSA) reductase (GlxR) activity, respectively, . Gcl condenses two molecules of glyoxylate to yield TSA, which is then reduced by GlxR to yield d-glycerate. GlxR displayed much greater specificity ( /K) for Gcl-derived TSA than it did for the TSA tautomer, hydroxypyruvate. This is relevant because TSA can potentially spontaneously tautomerize to yield hydroxypyruvate at neutral pH. However, kinetic and [H]-NMR evidence indicate that PA1501 (which encodes a putative hydroxypyruvate isomerase, Hyi) increases the rate of the Gcl-catalysed reaction, possibly by minimizing the impact of this unwanted tautomerization. Finally, we use X-ray crystallography to show that apo-GlxR is a configurationally flexible enzyme that can adopt two distinct tetrameric assemblies .

PubMed: 41369682
DOI: 10.1099/mic.0.001635

実験手法

X-RAY DIFFRACTION (2.21 Å)