Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.

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ID: 74701
2019
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Abstract
Mycobacterium tuberculosis is the cause of the world's most deadly infectious disease. Efforts are underway to target the methionine biosynthesis pathway, as it is not part of the host metabolism. The homoserine transacetylase MetX converts L-homoserine to O-acetyl-L-homoserine at the committed step of this pathway. In order to facilitate structure-based drug design, we determined the high-resolution crystal structures of three MetX proteins, including M. tuberculosis (MtMetX), Mycolicibacterium abscessus (MaMetX), and Mycolicibacterium hassiacum (MhMetX). A comparison of homoserine transacetylases from other bacterial and fungal species reveals a high degree of structural conservation amongst the enzymes. Utilizing homologous structures with bound cofactors, we analyzed the potential ligandability of MetX. The deep active-site tunnel surrounding the catalytic serine yielded many consensus clusters during mapping, suggesting that MtMetX is highly druggable.
Reference Key
chaton2019structuralscientific Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Chaton, Catherine T;Rodriguez, Emily S;Reed, Robert W;Li, Jian;Kenner, Cameron W;Korotkov, Konstantin V;
Journal Scientific reports
Year 2019
DOI
10.1038/s41598-019-56722-2
URL
Keywords
Mycobacterium tuberculosis mucormycosis motor vehicle accident immunocompetent necrotising fasciitis

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