Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-03-01

AUTHORS

Byron DeLaBarre, Paul R. Thompson, Gerard D. Wright, Albert M. Berghuis

ABSTRACT

The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry. More... »

PAGES

nsb0300_238

References to SciGraph publications

  • 1978-11. The taxonomy of binding sites in proteins in MOLECULAR AND CELLULAR BIOCHEMISTRY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/73359

    DOI

    http://dx.doi.org/10.1038/73359

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1031847470

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10700284


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