2PL5

Crystal Structure of Homoserine O-acetyltransferase from Leptospira interrogans

Summary for 2PL5

• Entry DOI: 10.2210/pdb2pl5/pdb
• Descriptor: Homoserine O-acetyltransferase, GLYCEROL (3 entities in total)
• Functional Keywords: homoserine o-acetyltransferase, alpha/beta hydrolase superfamily, transferase
• Biological source: Leptospira interrogans
• Cellular location: Cytoplasm (By similarity): Q8F4I0
• Total number of polymer chains: 1
• Total formula weight: 40340.47

Authors

Liu, L.,Wang, M.,Wang, Y.,Wei, Z.,Xu, H.,Gong, W. (deposition date: 2007-04-19, release date: 2007-11-20, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)