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Structure paper

TitleStructural roles of biocovalent flaninylation in berberine bridge enzyme
Journal, issue, pagesto be published
Publish dateJan 17, 2009 (structure data deposition date)
AuthorsWinkler, A. / Motz, K. / Riedl, S. / Puhl, M. / Macheroux, P. / Gruber, K.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.489 - 1.825 Å
Structure data

PDB-3fw7:
Structure of berberine bridge enzyme, H104A variant
Method: X-RAY DIFFRACTION / Resolution: 1.825 Å

PDB-3fw8:
Structure of berberine bridge enzyme, C166A variant
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3fw9:
Structure of berberine bridge enzyme in complex with (S)-scoulerine
Method: X-RAY DIFFRACTION / Resolution: 1.489 Å

PDB-3fwa:
Structure of berberine bridge enzyme, C166A variant in complex with (S)-reticuline
Method: X-RAY DIFFRACTION / Resolution: 1.496 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SLX:
(13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol / alkaloid*YM

ChemComp-REN:
(S)-reticuline / alkaloid*YM

Source
  • eschscholzia californica (California poppy)
KeywordsFLAVOPROTEIN / BI-COVALENT FLAVINYLATION / N-GLYCOSYLATION / ALAKLOID BIOSYNTHESIS / OXIDOREDUCTASE / Alkaloid metabolism / Cytoplasmic vesicle / FAD / Glycoprotein

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