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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
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1993 (English)In: J Mol Biol, ISSN 0022-2836, Vol. 232, no 1, 192-212 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1993. Vol. 232, no 1, 192-212 p.
Keyword [en]
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
Identifiers
URN: urn:nbn:se:uu:diva-21227PubMedID: 8331657OAI: oai:DiVA.org:uu-21227DiVA: diva2:49000
Available from: 2006-12-15 Created: 2006-12-15 Last updated: 2011-01-16

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Olin, BMannervik, B

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