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TitleInsight Into Coenzyme a Cofactor Binding and the Mechanism of Acyl-Transfer in an Acylating Aldehyde Dehydrogenase from Clostridium Phytofermentans.
Journal, issue, pagesSci. Rep., Vol. 6, Page 22108-, Year 2016
Publish dateAug 27, 2013 (structure data deposition date)
AuthorsTuck, L.R. / Altenbach, K. / Ang, T.F. / Crawshaw, A.D. / Campopiano, D.J. / Clarke, D.J. / Marles-Wright, J.
External linksSci. Rep. / PubMed:26899032
MethodsX-ray diffraction
Resolution1.64 - 2.083 Å
Structure data

PDB-4c3s:
Structure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment
Method: X-RAY DIFFRACTION / Resolution: 1.64 Å

PDB-5dbv:
Structure of a C269A mutant of propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-5dru:
Structure of His387Ala mutant of the propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment
Method: X-RAY DIFFRACTION / Resolution: 2.083 Å

Chemicals

ChemComp-SO4:
SULFATE ION

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

ChemComp-HOH:
WATER

ChemComp-COA:
COENZYME A

ChemComp-ACT:
ACETATE ION

Source
  • clostridium phytofermentans (bacteria)
  • clostridium phytofermentans (strain atcc 700394 / dsm 18823 / isdg) (bacteria)
KeywordsOXIDOREDUCTASE / Acylating aldehyde dehydrogenase / CoA / propionaldehyde / BMC / bacterial microcompartment

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