Summary for 5UGR
| Entry DOI | 10.2210/pdb5ugr/pdb |
| Descriptor | Malyl-CoA lyase/beta-methylmalyl-CoA lyase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | lyase |
| Biological source | Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) |
| Total number of polymer chains | 1 |
| Total formula weight | 37025.74 |
| Authors | Gonzalez, J.M. (deposition date: 2017-01-09, release date: 2017-02-08, Last modification date: 2023-10-04) |
| Primary citation | 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 Cited by 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: 28177317DOI: 10.1107/S2053230X17001029 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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