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Structure paper

TitleStructural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase.
Journal, issue, pagesBiochemistry, Vol. 57, Page 654-662, Year 2018
Publish dateAug 4, 2017 (structure data deposition date)
AuthorsMiller, B.R. / Kung, Y.
External linksBiochemistry / PubMed:29224355
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-5wpj:
Structure of the class II 3-hydroxy-3-methylglutaryl-CoA reductase from Streptococcus pneumoniae bound to NADPH in open conformations
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5wpk:
Structure of the class II 3-hydroxy-3-methylglutaryl-CoA reductase from Streptococcus pneumoniae bound to HMG-CoA and in a partially closed conformation
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

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

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-HMG:
3-HYDROXY-3-METHYLGLUTARYL-COENZYME A

ChemComp-PE4:
2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / precipitant*YM

Source
  • streptococcus pneumoniae (bacteria)
KeywordsOXIDOREDUCTASE / 3-hydroxy-3-methylglutaryl-CoA reductase / HMG-CoA / conformational change

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