Sagong_2019_Biochem.Biophys.Res.Commun_517_399

Reference

Title : Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420 - Sagong_2019_Biochem.Biophys.Res.Commun_517_399
Author(s) : Sagong HY , Hong J , Kim KJ
Ref : Biochemical & Biophysical Research Communications , 517 :399 , 2019
Abstract : Mycobacterium smegmatis is a good model for studying the physiology and pathogenesis of Mycobacterium tuberculosis due to its genetic similarity. As methionine biosynthesis exists only in microorganisms, the enzymes involved in methionine biosynthesis can be a potential target for novel antibiotics. Homoserine O-acetyltransferase from M. smegmatis (MsHAT) catalyzes the transfer of acetyl-group from acetyl-CoA to homoserine. To investigate the molecular mechanism of MsHAT, we determined its crystal structure in apo-form and in complex with either CoA or homoserine and revealed the substrate binding mode of MsHAT. A structural comparison of MsHAT with other HATs suggests that the conformation of the alpha5 to alpha6 region might influence the shape of the dimer. In addition, the active site entrance shows an open or closed conformation and might determine the substrate binding affinity of HATs.
ESTHER : Sagong_2019_Biochem.Biophys.Res.Commun_517_399
PubMedSearch : Sagong_2019_Biochem.Biophys.Res.Commun_517_399
PubMedID: 31378370
Gene_locus related to this paper: mycs2-metx

Related information

Gene_locus related to this paper: mycs2-metx

Citations formats

Sagong HY, Hong J, Kim KJ (2019)
Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420
Biochemical & Biophysical Research Communications 517 :399

Sagong HY, Hong J, Kim KJ (2019)
Biochemical & Biophysical Research Communications 517 :399