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Updated: Jul 11, 2026
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Published on: July 5, 2018
Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans
Mingzhu Wang1, Lin Liu, Yanli Wang
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, PR China.
Abstract:
Homoserine O-acetyltransferase (HTA, EC 2.3.1.31) initiates methionine biosynthesis pathway by catalyzing the transfer of acetyl group from acetyl-CoA to homoserine. This study reports the crystal structure of HTA from Leptospira interrogans determined at 2.2A resolution using selenomethionyl single-wavelength anomalous diffraction method. HTA is modular and consists of two structurally distinct domains--a core alpha/beta domain containing the catalytic site and a helical bundle called the lid domain. Overall, the structure fold belongs to alpha/beta hydrolase superfamily with the characteristic 'catalytic triad' residues in the active site. Detailed structure analysis showed that the catalytic histidine and serine are both present in two conformations, which may be involved in the catalytic mechanism for acetyl transfer.
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