5N00

Crystal structure of the decarboxylase AibA/AibB C56A variant

Summary for 5N00

• Entry DOI: 10.2210/pdb5n00/pdb
• Descriptor: Glutaconate CoA-transferase family, subunit A, Glutaconate CoA-transferase family, subunit B, ACETATE ION, ... (4 entities in total)
• Functional Keywords: decarboxylase, coa transferase like fold, lyase
• Biological source: Myxococcus xanthus (strain DK 1622); More
• Total number of polymer chains: 4
• Total formula weight: 109292.33

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

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: 28508504
DOI: 10.1002/anie.201701992

Experimental method

X-RAY DIFFRACTION (1.9 Å)