3SXX

Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)

Summary for 3SXX

• Entry DOI: 10.2210/pdb3sxx/pdb
• Related: 1A2V 2OOV 3SX1
• Descriptor: Peroxisomal primary amine oxidase, COBALT (II) ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: oxidoreductase, peroxisome
• Biological source: Pichia angusta (Yeast)
• Cellular location: Peroxisome: P12807
• Total number of polymer chains: 6
• Total formula weight: 470299.28

Authors

Klema, V.J.,Wilmot, C.M. (deposition date: 2011-07-15, release date: 2012-05-02, Last modification date: 2024-11-06)

Primary citation

Klema, V.J.,Johnson, B.J.,Klinman, J.P.,Wilmot, C.M.
The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.
Acta Crystallogr.,Sect.F, 68:501-510, 2012

PubMed Abstract: Copper amine oxidases (CAOs) catalyze the oxidative deamination of primary amines to their corresponding aldehydes, with the concomitant reduction of O(2) to H(2)O(2). Catalysis requires two cofactors: a mononuclear copper center and the cofactor 2,4,5-trihydroxyphenylalanine quinone (TPQ). TPQ is synthesized through the post-translational modification of an endogenous tyrosine residue and requires only oxygen and copper to proceed. TPQ biogenesis in CAO can be supported by alternate metals, albeit at decreased rates. A variety of factors are thought to contribute to the degree to which a metal can support TPQ biogenesis, including Lewis acidity, redox potential and electrostatic stabilization capability. The crystal structure has been solved of one of two characterized CAOs from the yeast Hansenula polymorpha (HPAO-1) in its metal-free (apo) form, which contains an unmodified precursor tyrosine residue instead of fully processed TPQ (HPAO-1 was denoted HPAO in the literature prior to 2010). Structures of apoHPAO-1 in complex with Cu(I) and Co(II) have also been solved, providing structural insight into metal binding prior to biogenesis.

PubMed: 22691777
DOI: 10.1107/S1744309112012857

Experimental method

X-RAY DIFFRACTION (1.27 Å)