2f0x
From Proteopedia
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Crystal structure and function of human thioesterase superfamily member 2(THEM2)
Overview
Hotdog-fold has been identified in more than 1000 proteins, yet many of, which in eukaryotes are less studied. No structural or functional studies, of human thioesterase superfamily member 2 (hTHEM2) have been reported, before. Since hTHEM2 exhibits about 20% sequence identity to Escherichia, coli PaaI protein, it was proposed to be a thioesterase with a, hotdog-fold. Here, we report the crystallographic structure of recombinant, hTHEM2, determined by the single-wavelength anomalous dispersion method at, 2.3A resolution. This structure 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.
About this Structure
2F0X is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of human thioesterase superfamily member 2., Cheng Z, Song F, Shan X, Wei Z, Wang Y, Dunaway-Mariano D, Gong W, Biochem Biophys Res Commun. 2006 Oct 13;349(1):172-7. Epub 2006 Aug 14. PMID:16934754
Page seeded by OCA on Mon Nov 12 21:57:57 2007
Categories: Homo sapiens | Single protein | Cheng, Z. | Gong, W. | Shan, X. | Song, F. | Wang, Y. | Wei, Z. | SO4 | Hot dog fold
