5w8o

Homoserine transacetylase MetX from Mycobacterium hassiacum

spinqualitylabelsall models 5w8o, resolution 1.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5w8o is a 2 chain structure with sequence from Mycolicibacterium hassiacum DSM 44199. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.47Å Ligands: CA, GOL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K5B926_MYCHD Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.[HAMAP-Rule:MF_00296] Publication Abstract from PubMed 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. Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.,Chaton CT, Rodriguez ES, Reed RW, Li J, Kenner CW, Korotkov KV Sci Rep. 2019 Dec 30;9(1):20267. doi: 10.1038/s41598-019-56722-2. PMID:31889085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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