6OGM

Crystal structure of apo unFused 4-OT

6OGM の概要

• エントリーDOI: 10.2210/pdb6ogm/pdb
• 関連するPDBエントリー: 6BLM
• 分子名称: 4-oxalocrotonate tautomerase, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 79559.20

構造登録者

Medellin, B.P.,Whitman, C.P.,Zhang, Y.J. (登録日: 2019-04-03, 公開日: 2020-02-26, 最終更新日: 2023-10-25)

主引用文献

Baas, B.J.,Medellin, B.P.,LeVieux, J.A.,de Ruijter, M.,Zhang, Y.J.,Brown, S.D.,Akiva, E.,Babbitt, P.C.,Whitman, C.P.
Structural, Kinetic, and Mechanistic Analysis of an Asymmetric 4-Oxalocrotonate Tautomerase Trimer.
Biochemistry, 58:2617-2627, 2019

PubMed Abstract: A 4-oxalocrotonate tautomerase (4-OT) trimer has been isolated from Burkholderia lata, and a kinetic, mechanistic, and structural analysis has been performed. The enzyme is the third described oligomer state for 4-OT along with a homo- and heterohexamer. The 4-OT trimer is part of a small subset of sequences (133 sequences) within the 4-OT subgroup of the tautomerase superfamily (TSF). The TSF has two distinct features: members are composed of a single β-α-β unit (homo- and heterohexamer) or two consecutively joined β-α-β units (trimer) and generally have a catalytic amino-terminal proline. The enzyme, designated as fused 4-OT, functions as a 4-OT where the active site groups (Pro-1, Arg-39, Arg-76, Phe-115, Arg-127) mirror those in the canonical 4-OT from Pseudomonas putida mt-2. Inactivation by 2-oxo-3-pentynoate suggests that Pro-1 of fused 4-OT has a low p K enabling the prolyl nitrogen to function as a general base. A remarkable feature of the fused 4-OT is the absence of P3 rotational symmetry in the structure (1.5 Å resolution). The asymmetric arrangement of the trimer is not due to the fusion of the two β-α-β building blocks because an engineered "unfused" variant that breaks the covalent bond between the two units (to generate a heterohexamer) assumes the same asymmetric oligomerization state. It remains unknown how the different active site configurations contribute to the observed overall activities and whether the asymmetry has a biological purpose or role in the evolution of TSF members.

PubMed: 31074977
DOI: 10.1021/acs.biochem.9b00303

実験手法

X-RAY DIFFRACTION (1.865 Å)