Crystal Structure of Human Thioesterase Superfamily Member 2.
From: School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
Biochemical and biophysical research communications
- Publish Date: Oct 2006
- ISSN: 0006-291X
- Volume: 349
- Issue: 1
- Pages: 172-7
- Medium: Print
- Language: English
- Citation (JAMA): Cheng Zhongjun, Song Feng, Shan Xiaoyue, et al. Crystal Structure of Human Thioesterase Superfamily Member 2.. Biochem. Biophys. Res. Commun. Oct 2006;349:172-7
Abstract
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.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Escherichia coli, Humans, Kinetics, Molecular Sequence Data, Protein Conformation, Protein Folding, Protein Structure, Secondary, Sequence Homology, Amino Acid, Substrate Specificity, Thiolester Hydrolases
Check for Full Text / PubMed Unique Identifier (PMID): 16934754
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.