Creative Biostructure

Online Inquiry

Please enter "biostructure" as the verification code.

THEM2 Protein Crystal

(CBCRY16)  Download Datasheet
Background
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
Gene ID
55856
Chromosome Location
6p22.2
Function
hydrolase activity
Reference
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