Document Detail


Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
MedLine Citation:
PMID:  8331657     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
Authors:
I Sinning; G J Kleywegt; S W Cowan; P Reinemer; H W Dirr; R Huber; G L Gilliland; R N Armstrong; X Ji; P G Board
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  232     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1993 Jul 
Date Detail:
Created Date:  1993-08-19     Completed Date:  1993-08-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  192-212     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology, Uppsala University Biomedical Center, Sweden.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Crystallography
Glutathione / chemistry
Glutathione Transferase / classification,  ultrastructure*
Humans
Macromolecular Substances
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Sequence Alignment
Software
X-Ray Diffraction
Chemical
Reg. No./Substance:
0/Macromolecular Substances; 0/Recombinant Proteins; 70-18-8/Glutathione; EC 2.5.1.18/Glutathione Transferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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