Structural highlights
Publication Abstract from PubMedMalyl-CoA lyase (MCL) is an Mg2+-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 A resolution X-ray crystal structure of MCL from Methylobacterium extorquens AM1 with bound Mg2+ is presented. Structural alignment with the closely related Rhodobacter sphaeroides 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 degrees 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. Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.,Gonzalez JM, Marti-Arbona R, Chen JC, Unkefer CJ Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):79-85. doi:, 10.1107/S2053230X17001029. Epub 2017 Jan 27. PMID:28177317[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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