1W7C

PPLO at 1.23 Angstroms

1W7C の概要

• エントリーDOI: 10.2210/pdb1w7c/pdb
• 関連するPDBエントリー: 1N9E
• 分子名称: LYSYL OXIDASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (9 entities in total)
• 機能のキーワード: amine oxidase, oxidoreductase, quinoprotein, topaquinone enzyme
• 由来する生物種: PICHIA PASTORIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 87272.08

構造登録者

Duff, A.P.,Cohen, A.E.,Ellis, P.J.,Guss, J.M. (登録日: 2004-09-01, 公開日: 2006-08-31, 最終更新日: 2025-10-01)

主引用文献

Duff, A.P.,Cohen, A.E.,Ellis, P.J.,Hilmer, K.,Langley, D.B.,Dooley, D.M.,Freeman, H.C.,Guss, J.M.
The 1.23 A Structure of Pichia Pastoris Lysyl Oxidase Reveals a Lysine-Lysine Cross-Link
Acta Crystallogr.,Sect.D, 62:1073-, 2006

PubMed Abstract: The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 Angstrom resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the CuAO enzyme family in having the ability to oxidize the side chain of lysine residues in a polypeptide. In the asymmetric unit of the crystals, the structure analysis has located residues 43-779 of the polypeptide chain, seven carbohydrate residues, the active-site Cu atom, an imidazole molecule bound at the active site, two buried Ca(2+) ions, five surface Mg(2+) ions, five surface Cl(-) ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and R(free) = 0.146. The TPQ cofactor and several other active-site residues are poorly ordered, in contrast to the surrounding well ordered structure. A covalent cross-link is observed between two lysine residues, Lys778 and Lys66. The cross-link is likely to have been formed by the oxidation of Lys778 followed by a spontaneous reaction with Lys66. The link is modelled as dehydrolysinonorleucine.

PubMed: 16929109
DOI: 10.1107/S0907444906026333

実験手法

X-RAY DIFFRACTION (1.23 Å)