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Crystal structure of the essential biotin-dependent carboxylase AccA3 from Mycobacterium tuberculosis
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 2
2017 (English)In: FEBS Open Bio, E-ISSN 2211-5463, Vol. 7, no 5, 620-626 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2017. Vol. 7, no 5, 620-626 p.
Keyword [en]
drug design, FASII, lipid metabolism, Rv3285, tuberculosis, tyrosine
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-143398DOI: 10.1002/2211-5463.12212ISI: 000400300000001PubMedID: 28469974OAI: oai:DiVA.org:su-143398DiVA: diva2:1104062
Available from: 2017-05-31 Created: 2017-05-31 Last updated: 2017-05-31Bibliographically approved

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