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PDBsum entry 2pl5
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References listed in PDB file
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Key reference
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Title
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Crystal structure of homoserine o-Acetyltransferase from leptospira interrogans.
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Authors
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M.Wang,
L.Liu,
Y.Wang,
Z.Wei,
P.Zhang,
Y.Li,
X.Jiang,
H.Xu,
W.Gong.
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Ref.
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Biochem Biophys Res Commun, 2007,
363,
1050-1056.
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PubMed id
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Abstract
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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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