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Product Summary
Fragment
Full length
Protein Description
Thioesterase superfamily member 2
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.
Protein Classification
Hydrolase
Structure Weight
132969.96 Da
PDBID
2F0X
Method
X-Ray Diffraction
Resolution
2.3Å
Ligand Chemical Component
sulfate ion
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
cDNALength
528