5MZY
Crystal structure of the decarboxylase AibA/AibB in complex with a possible transition state analog
Summary for 5MZY
| Entry DOI | 10.2210/pdb5mzy/pdb |
| Descriptor | Glutaconate CoA-transferase family, subunit A, Glutaconate CoA-transferase family, subunit B, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | decarboxylase, coa transferase like fold, transition state analog, lyase |
| Biological source | Myxococcus xanthus (strain DK 1622) More |
| Total number of polymer chains | 4 |
| Total formula weight | 110068.27 |
| Authors | Bock, T.,Luxenburger, E.,Hoffmann, J.,Schuetza, V.,Feiler, C.,Mueller, R.,Blankenfeldt, W. (deposition date: 2017-02-02, release date: 2017-05-31, Last modification date: 2024-01-17) |
| Primary citation | Bock, T.,Luxenburger, E.,Hoffmann, J.,Schutza, V.,Feiler, C.,Muller, R.,Blankenfeldt, W. AibA/AibB Induces an Intramolecular Decarboxylation in Isovalerate Biosynthesis by Myxococcus xanthus. Angew. Chem. Int. Ed. Engl., 56:9986-9989, 2017 Cited by PubMed Abstract: Isovaleryl coenzyme A (IV-CoA) is an important precursor for iso-fatty acids and lipids. It acts in the development of myxobacteria, which can produce this compound from acetyl-CoA through alternative IV-CoA biosynthesis (aib). A central reaction of aib is catalyzed by AibA/AibB, which acts as a cofactor-free decarboxylase despite belonging to the family of CoA-transferases. We developed an efficient expression system for AibA/AibB that allowed the determination of high-resolution crystal structures in complex with different ligands. Through mutational studies, we show that an active-site cysteine previously proposed to be involved in decarboxylation is not required for activity. Instead, AibA/AibB seems to induce an intramolecular decarboxylation by binding its substrate in a hydrophobic cavity and forcing it into a bent conformation. Our study opens opportunities for synthetic biology studies, since AibA/AibB may be suitable for the production of isobutene, a precursor of biofuels and chemicals. PubMed: 28508504DOI: 10.1002/anie.201701992 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
