Structure of m>Methylobacterium extorquensm> malyl-CoA lyase: CoA-substrate binding correlates with domain shift

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• 作者：Javier M. Gonzá ; lez ; Ricardo Marti-Arbona ; Julian C.-H. Chen and Clifford J. Unkefer
• 关键词：biofuels ; metabolic engineering ; methanol ; malyl-CoA lyase ; Methylobacterium extorquens
• 刊名：Acta Crystallographica Section F
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：73
• 期：2
• 页码：79-85
• 全文大小：1327K
• ISSN：1744-3091

文摘

Malyl-CoA lyase (MCL) is an Mg²⁺-dependent enzyme that catalyzes the reversible cleavage of (2m>Sm>)-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 m>Methylobacterium extorquensm> AM1 with bound Mg²⁺ is presented. Structural alignment with the closely related m>Rhodobacter sphaeroidesm> malyl-CoA lyase complexed with Mg²⁺, 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.