1w7c

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Revision as of 21:22, 24 November 2007

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spinqualitylabelsall models 1w7c, resolution 1.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PPLO AT 1.23 ANGSTROMS

Overview

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.

About this Structure

1W7C is a Single protein structure of sequence from Pichia pastoris with NAG, CU, CA, MG, CL, TPQ and IMD as ligands. Active as Protein-lysine 6-oxidase, with EC number 1.4.3.13 Full crystallographic information is available from OCA.

Reference

The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link., Duff AP, Cohen AE, Ellis PJ, Hilmer K, Langley DB, Dooley DM, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1073-84. Epub 2006, Aug 19. PMID:16929109

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