6JVW

Crystal structure of maleylpyruvate hydrolase from Sphingobium sp. SYK-6 in complex with manganese (II) ion and pyruvate

6JVW の概要

• エントリーDOI: 10.2210/pdb6jvw/pdb
• 分子名称: maleylpyruvate hydrolase, PYRUVIC ACID, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Sphingobium sp. (strain NBRC 103272 / SYK-6)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67074.44

構造登録者

Hong, H.,Kim, K.-J. (登録日: 2019-04-17, 公開日: 2019-05-29, 最終更新日: 2023-11-22)

主引用文献

Hong, H.,Seo, H.,Kim, K.J.
Structural insights into a maleylpyruvate hydrolase from sphingobium sp. SYK-6, a bacterium degrading lignin-derived aryls.
Biochem.Biophys.Res.Commun., 514:765-771, 2019

PubMed Abstract: Sphingobium sp. strain SYK-6, an aerobic gram-negative bacillus found in soil, is known for utilizing lignin-derived monoaryls and biaryls as carbon sources and degrading aromatic compounds. The Sphingobium sp. strain SYK-6 genome contains three genes involved in salicylate catabolism: SLG_11260, SLG_11270, and SLG_11280. Here, we report that the gene product of SLG_11280 functions as a maleylpyruvate hydrolase (SsMPH) with K and K values of 166.2 μM and 3.76 min, respectively. This study also reveals the crystal structures of both the apo and pyruvate-manganese ion-bound SsMPH, which revealed that like other fumarylacetoacetate hydrolases, SsMPH dimerizes and has nine unique 3-helices. Molecular docking studies of maleylpyruvate also revealed the likely binding mode of SsMPH and its substrate.

PubMed: 31079929
DOI: 10.1016/j.bbrc.2019.05.030

実験手法

X-RAY DIFFRACTION (2.25 Å)