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Structure paper

TitleCrystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH.
Journal, issue, pagesProteins, Vol. 80, Page 1250-1257, Year 2012
Publish dateJun 21, 2011 (structure data deposition date)
AuthorsDutta, D. / Bhattacharyya, S. / Das, A.K.
External linksProteins / PubMed:22275129
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-3sj7:
Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus subsp. aureus (bacteria)
KeywordsOXIDOREDUCTASE / ketoreductase / Rossmann fold

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