3NBB: Crystal Structure Of Mutant Y305f Expressed In E. Coli In The Copper Amine Oxidase From Hansenula Polymorpha

The copper amine oxidases carry out two copper-dependent processes: production of their own redox-active cofactor (2,4,5-trihydroxyphenylalanine quinone, TPQ) and the subsequent oxidative deamination of substrate amines. Because the same active site pocket must facilitate both reactions, individual active site residues may serve multiple roles. We have examined the roles of a strictly conserved active site tyrosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetically, spetroscopically (Dubois and Klinman (2006) Biochemistry 45, 3178), and, in the present work, structurally. While the Y305A enzyme is almost identical to the wild type, a novel, highly oxygenated species replaces TPQ in the Y305F active sites. This new structure not only provides the first direct detection of peroxy intermediates in cofactor biogenesis but also indicates the critical control of oxidation chemistry that can be conferred by a single active site residue.
PDB ID: 3NBBDownload
MMDB ID: 84942
PDB Deposition Date: 2010/6/3
Updated in MMDB: 2010/09
Experimental Method:
x-ray diffraction
Resolution: 2.05  Å
Source Organism:
Similar Structures:
Biological Unit for 3NBB: dimeric; determined by author and by software (PISA)
Molecular Components in 3NBB
Label Count Molecule
Proteins (2 molecules)
Peroxisomal Primary Amine Oxidase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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