2PL5

Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans

2PL5 の概要

• エントリーDOI: 10.2210/pdb2pl5/pdb
• 分子名称: Homoserine O-acetyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: homoserine o-acetyltransferase, alpha/beta hydrolase superfamily, transferase
• 由来する生物種: Leptospira interrogans
• 細胞内の位置: Cytoplasm (By similarity): Q8F4I0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40340.47

構造登録者

Liu, L.,Wang, M.,Wang, Y.,Wei, Z.,Xu, H.,Gong, W. (登録日: 2007-04-19, 公開日: 2007-11-20, 最終更新日: 2024-03-13)

主引用文献

Wang, M.,Liu, L.,Wang, Y.,Wei, Z.,Zhang, P.,Li, Y.,Jiang, X.,Xu, H.,Gong, W.
Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans
Biochem.Biophys.Res.Commun., 363:1050-1056, 2007

PubMed 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.

PubMed: 17927957
DOI: 10.1016/j.bbrc.2007.08.153

実験手法

X-RAY DIFFRACTION (2.2 Å)