Journal:FEBS Open Bio:1

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis Matthew Bennett, Martin Högbom Molecular Tour Biotin-dependent acetyl-CoA carboxylases catalyze the committed step in type II fatty acid biosynthesis, the main route for production of membrane phospholipids in bacteria, and are considered a key target for antibacterial drug discovery. Here we describe the first structure of AccA3, an essential component of the acetyl-CoA carboxylase system in Mycobacterium tuberculosis (MTb). The structure, sequence comparisons, and modeling of ligand-bound states reveal that the ATP cosubstrate-binding site shows distinct differences compared to other bacterial and eukaryotic biotin carboxylases, including all human homologs. This suggests the possibility to design MTb AccA3 subtype-specific inhibitors. Mycobacterium tuberculosis AccA3 adopts the ATPgrasp superfamily fold, and crystallized as a dimer in the asymmetric unit. The lack of an ordered structure for domain B in chain B.

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky