3T0U

Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I)

3T0U の概要

• エントリーDOI: 10.2210/pdb3t0u/pdb
• 関連するPDBエントリー: 2OOV 3SX1 3SXX
• 分子名称: Peroxisomal primary amine oxidase, COPPER (I) ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, peroxisome
• 由来する生物種: Pichia angusta (Yeast)
• 細胞内の位置: Peroxisome: P12807
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 234933.25

構造登録者

Klema, V.J.,Wilmot, C.M. (登録日: 2011-07-20, 公開日: 2012-05-02, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)