Cat. No.

CBCRY16

Background

The crystallographic structure of recombinant hTHEM2, determined by the single-wavelength anomalous dispersion method at 2.3A resolution, demonstrates that hTHEM2 indeed contains a hotdog-fold and forms a back-to-back tetramer as other hotdog proteins. Based on structural and sequence conservation, the thioesterase active site in hTHEM2 is predicted. The structure and substrate specificity are most similar to those of the bacterial phenylacetyl-CoA hydrolase. Asp65, located on the central alpha-helix of subunit B, was shown by site-directed mutagenesis to be essential to catalysis.

Molecular description

Protein Classification

Hydrolase

Structure Weight

132969.96 Da

Polymer

1

Molecule

Thioesterase superfamily member 2 

Chain Length

176 amino acids

Crystal Description

PDB ID

2F0X

MMDB ID

42159

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.3Å

Ligand Chemical Component

sulfate ion

Gene information

Gene Name

THEM2

Synonyms

HT012; MGC4961; PNAS-27; 15 Kd protein; OTTHUMP00000016090; OTTHUMP00000039398; hypothalamus protein HT012

UniProt ID

Q9NPJ3

GeneID

55856

Chromosome  Location

6p22.2

Function

hydrolase activity

Reference

Cheng, Z.,  Song, F.,  Shan, X.,  Wei, Z.,  Wang, Y.,  Dunaway-Mariano, D.,  Gong, W. (2006) Crystal structure of human thioesterase superfamily member 2 Biochem.Biophys.Res.Commun. 349: 172-177