Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.

Content Provider	Semantic Scholar
Author	González, Javier M. Martí-Arbona, Ricardo Chen, Julian C-H Unkefer, Clifford J.
Copyright Year	2017
Abstract	Malyl-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 Å 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° 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.
Starting Page	79
Ending Page	85
Page Count	7
File Format	PDF HTM / HTML
DOI	10.1107/S2053230X17001029
PubMed reference number	28177317
Journal	Medline
Volume Number	73
Part	2
Alternate Webpage(s)	http://journals.iucr.org/f/issues/2017/02/00/nj5268/nj5268.pdf
Alternate Webpage(s)	https://doi.org/10.1107/S2053230X17001029
Journal	Acta crystallographica. Section F, Structural biology communications
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article