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TitleStructures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism
Journal, issue, pagesBiochem. J., Vol. 449, Page 79-89, Year 2013
Publish dateApr 25, 2012 (structure data deposition date)
AuthorsHu, K. / Zhao, M. / Zhang, T. / Zha, M. / Zhong, C. / Jiang, Y. / Ding, J.
External linksBiochem. J. / PubMed:23050861
MethodsX-ray diffraction
Resolution2 - 3.02 Å
Structure data

PDB-4eue:
Crystal structure of Clostridium acetobutulicum trans-2-enoyl-CoA reductase in complex with NADH
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4euf:
Crystal structure of Clostridium acetobutulicum trans-2-enoyl-CoA reductase in complex with NAD
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4euh:
Crystal structure of Clostridium acetobutulicum trans-2-enoyl-CoA reductase apo form
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4fbg:
Crystal structure of Treponema denticola trans-2-enoyl-CoA reductase in complex with NAD
Method: X-RAY DIFFRACTION / Resolution: 3.02 Å

Chemicals

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

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

Source
  • clostridium acetobutylicum (bacteria)
  • treponema denticola (bacteria)
KeywordsOXIDOREDUCTASE / TER / biofuel / synthetic biology / reductase / catalytic mechanism / substrate specificity

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