3D2H

Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form

Summary for 3D2H

• Entry DOI: 10.2210/pdb3d2h/pdb
• Related: 3D2D 3D2J
• Descriptor: berberine bridge-forming enzyme, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: bi-covalent flavinylation, n-glycosylation, alakloid biosynthesis, p-cresol methylhydroxylase superfamily, oxidoreductase
• Biological source: Eschscholzia californica (California poppy)
• Cellular location: Cytoplasmic vesicle: P30986
• Total number of polymer chains: 1
• Total formula weight: 62930.27

Authors

Winkler, A.,Lyskowski, A.,Macheroux, P.,Gruber, K. (deposition date: 2008-05-08, release date: 2008-10-28, Last modification date: 2024-10-30)

Primary citation

Winkler, A.,Lyskowski, A.,Riedl, S.,Puhl, M.,Kutchan, T.M.,Macheroux, P.,Gruber, K.
A concerted mechanism for berberine bridge enzyme
Nat.Chem.Biol., 4:739-741, 2008

PubMed Abstract: Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor.

PubMed: 18953357
DOI: 10.1038/nchembio.123

Experimental method

X-RAY DIFFRACTION (1.65 Å)