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Structure paper

TitleThe structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 171, Page 89-99, Year 2021
Publish dateApr 21, 2020 (structure data deposition date)
AuthorsCaliandro, R. / Polsinelli, I. / Demitri, N. / Musiani, F. / Martens, S. / Benini, S.
External linksInt. J. Biol. Macromol. / PubMed:33412202
MethodsX-ray diffraction
Resolution1.2 - 1.4 Å
Structure data

PDB-6ysb:
Crystal structure of Malus domestica Double Bond Reductase (MdDBR) apo form
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-6ytz:
Crystal structure of Malus domestica Double Bond Reductase (MdDBR) in complex with NADPH
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6yux:
Crystal structure of Malus domestica Double Bond Reductase (MdDBR) ternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.36 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGR:
R-1,2-PROPANEDIOL

ChemComp-NA:
Unknown entry

ChemComp-FER:
3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID

Source
  • pyrus ussuriensis x pyrus communis (plant)
  • malus domestica (apple)
KeywordsBIOSYNTHETIC PROTEIN / phenylpropanoid pathway / double bond reductase / Malus domestica

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