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Structure paper

TitleCrystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Journal, issue, pagesTo be Published
Publish dateJul 20, 2013 (structure data deposition date)
AuthorsFischer, B. / Branlant, G. / Talfournier, F. / Gruez, A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.5 - 1.55 Å
Structure data

PDB-4lrs:
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4lrt:
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-PYR:
PYRUVIC ACID

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-FOR:
FORMYL GROUP

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-COA:
COENZYME A

Source
  • thermomonospora curvata (bacteria)
KeywordsOXIDOREDUCTASE / Rossmann fold / TIM barrel domain / Dehydrogenase / aldolase / Lyase/OXIDOREDUCTASE / Rosmmann Fold / TIM barrel / Lyase-OXIDOREDUCTASE complex

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