5UGR

Malyl-CoA lyase from Methylobacterium extorquens

「4ROQ」から置き換えられました

5UGR の概要

• エントリーDOI: 10.2210/pdb5ugr/pdb
• 分子名称: Malyl-CoA lyase/beta-methylmalyl-CoA lyase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37025.74

構造登録者

Gonzalez, J.M. (登録日: 2017-01-09, 公開日: 2017-02-08, 最終更新日: 2023-10-04)

主引用文献

Gonzalez, J.M.,Marti-Arbona, R.,Chen, J.C.,Unkefer, C.J.
Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.
Acta Crystallogr F Struct Biol Commun, 73:79-85, 2017

PubMed Abstract: Malyl-CoA lyase (MCL) is an Mg-dependent enzyme that catalyzes the reversible cleavage of (2S)-4-malyl-CoA to yield acetyl-CoA and glyoxylate. MCL enzymes, which are found in a variety of bacteria, are members of the citrate lyase-like family and are involved in the assimilation of one- and two-carbon compounds. Here, the 1.56 Å resolution X-ray crystal structure of MCL from Methylobacterium extorquens AM1 with bound Mg is presented. Structural alignment with the closely related Rhodobacter sphaeroides malyl-CoA lyase complexed with Mg, oxalate and CoA allows a detailed analysis of the domain motion of the enzyme caused by substrate binding. Alignment of the structures shows that a simple hinge motion centered on the conserved residues Phe268 and Thr269 moves the C-terminal domain by about 30° relative to the rest of the molecule. This domain motion positions a conserved aspartate residue located in the C-terminal domain in the active site of the adjacent monomer, which may serve as a general acid/base in the catalytic mechanism.

PubMed: 28177317
DOI: 10.1107/S2053230X17001029

実験手法

X-RAY DIFFRACTION (1.56 Å)