5mlk

Publication Abstract from PubMed

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. DATABASE: Coordinates and structure factors have been deposited in the Protein Data Bank with the accession number 5MLK.

Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis.,Bennett M, Hogbom M FEBS Open Bio. 2017 Apr 4;7(5):620-626. doi: 10.1002/2211-5463.12212. eCollection, 2017 May. PMID:28469974^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.