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Structure of Methylobacterium extorquens malyl‐CoA lyase: CoA‐substrate binding correlates with domain shift
Author(s) -
González Javier M.,
Marti-Arbona Ricardo,
Chen Julian C.-H.,
Unkefer Clifford J.
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17001029
Subject(s) - lyase , stereochemistry , chemistry , glyoxylate cycle , methylobacterium , rhodobacter sphaeroides , active site , enzyme , residue (chemistry) , transferase , biochemistry , crystallography , photosynthesis , 16s ribosomal rna , gene
Malyl‐CoA lyase (MCL) is an Mg 2+ ‐dependent enzyme that catalyzes the reversible cleavage of (2 S )‐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 2+ is presented. Structural alignment with the closely related Rhodobacter sphaeroides malyl‐CoA lyase complexed with Mg 2+ , 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.