research papers
The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 Å 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 Ca2+ ions, five surface Mg2+ ions, five surface Cl- ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and Rfree = 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.
Keywords: copper proteins; amine oxidases; quinoproteins; topaquinone; lysyl oxidase; dehydrolysinonorleucine.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S0907444906026333/wd5066sup1.pdf |
PDB reference: PPLO, 1w7c, r1w7csf