PDBsum entry 2pl5

Transferase

PDB id: 2pl5

Contents

Protein chain

362 a.a. *

Ligands

GOL ×2

Waters ×188

* Residue conservation analysis

PDB id:

2pl5

Name:

Transferase

Title:

Crystal structure of homoserine o-acetyltransferase from leptospira interrogans

Structure:

Homoserine o-acetyltransferase. Chain: a. Synonym: homoserine o-trans-acetylase, homoserine transacetylase, hta. Engineered: yes

Source:

Leptospira interrogans. Organism_taxid: 173. Gene: metx. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.20Å R-factor: 0.218 R-free: 0.258

Authors:

L.Liu,M.Wang,Y.Wang,Z.Wei,H.Xu,W.Gong

Key ref:

M.Wang et al. (2007). Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans. Biochem Biophys Res Commun, 363, 1050-1056. PubMed id: 17927957

Date:

19-Apr-07 Release date: 20-Nov-07

Protein chain

Q8F4I0  (METXA_LEPIN) -  Homoserine O-acetyltransferase from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)

Seq: 366 a.a.

Struc: 362 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.31 - homoserine O-acetyltransferase.
• Reaction: L-homoserine + acetyl-CoA = O-acetyl-L-homoserine + CoA

L-homoserine + acetyl-CoA (Bound ligand (Het Group name = GOL) matches with 40.00% similarity) = O-acetyl-L-homoserine + CoA

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Biochem Biophys Res Commun 363:1050-1056 (2007)

PubMed id: 17927957

Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans.

M.Wang, L.Liu, Y.Wang, Z.Wei, P.Zhang, Y.Li, X.Jiang, H.Xu, W.Gong.

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.