2pl5 | pdb_00002pl5
Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans
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Overview
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.
About this Structure
2PL5 is a Single protein structure of sequence from Leptospira interrogans with GOL as ligand. Active as Homoserine O-acetyltransferase, with EC number 2.3.1.31 Full crystallographic information is available from OCA.
Reference
Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans., Wang M, Liu L, Wang Y, Wei Z, Zhang P, Li Y, Jiang X, Xu H, Gong W, Biochem Biophys Res Commun. 2007 Nov 30;363(4):1050-6. Epub 2007 Sep 4. PMID:17927957
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