5MLK

Biotin dependent carboxylase AccA3 dimer from Mycobacterium tuberculosis (Rv3285)

Summary for 5MLK

• Entry DOI: 10.2210/pdb5mlk/pdb
• Descriptor: Acetyl-COA carboxylase (2 entities in total)
• Functional Keywords: biotin dependant carboxylase, grasp, ligase
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 2
• Total formula weight: 130925.30

Authors

Bennett, M.D.,Hogbom, M. (deposition date: 2016-12-07, release date: 2017-03-08, Last modification date: 2024-05-08)

Primary citation

Bennett, M.,Hogbom, M.
Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis.
FEBS Open Bio, 7:620-626, 2017

PubMed Abstract: 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 (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.

PubMed: 28469974
DOI: 10.1002/2211-5463.12212

Experimental method

X-RAY DIFFRACTION (1.939 Å)