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Quaternary assembly and crystal structure of GDP-d-mannose 4,6 dehydratase fromParamecium bursaria Chlorellavirus

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
339
Issue
1
Identifiers
DOI: 10.1016/j.bbrc.2005.11.009
Keywords
  • Paramecium Bursaria Chlorellavirus Enzyme
  • Gdp-D-Mannose Dehydratase
  • Protein Structure
  • Quaternary Assembly
  • Gdp-L-Fucose Biosynthesis
Disciplines
  • Biology

Abstract

Abstract GDP- d-mannose 4,6 dehydratase is the first enzyme in the de novo biosynthetic pathway of GDP- l-fucose, the activated form of l-fucose, a monosaccharide found in organisms ranging from bacteria to mammals. We determined the three-dimensional structure of GDP- d-mannose 4,6 dehydratase from the Paramecium bursaria Chlorella virus at 3.8 Å resolution. Unlike other viruses that use the host protein machinery to glycosylate their proteins, P. bursaria Chlorella virus modifies its structural proteins using many glycosyltransferases, being the first virus known to encode enzymes involved in sugar metabolism. P. bursaria Chlorella virus GDP- d-mannose 4,6 dehydratase belongs to the short-chain dehydrogenase/reductase protein superfamily. Accordingly, the family fold and the specific Thr, Tyr, and Lys catalytic triad are well conserved in the viral enzyme.

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