Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 Å resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture

Journal of Molecular Biology

Volumn 255, Issue 2, 1996, Pages 289-309

  Reinemer, Peter ^a,b   Prade, Lars ^b   Hof, Peter ^b   Neuefeind, Torsten ^a,b   Huber, Robert ^b   Zettl, Rolf ^c   Palme, Klaus ^c   Schell, Jeff ^c   Koelln, Ingo ^d   Bartunik, Hans D ^d   Bieseler, Barbara ^a  

^a BAYER AG   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

^d MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

Author keywords

crystallography; glutathione S transferase; glutathione binding domain; herbicide detoxification; protein structure

Indexed keywords

DIMER; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HERBICIDE; S HEXYLGLUTATHIONE; VEGETABLE PROTEIN;

ARABIDOPSIS; ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; ENZYME STRUCTURE; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ARABIDOPSIS THALIANA;

EID: 0029914965     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0024     Document Type: Article

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