1n9e

From Proteopedia

---

Revision as of 20:38, 24 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1n9e, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PICHIA PASTORIS LYSYL OXIDASE PPLO

Overview

Pichia pastoris lysyl oxidase (PPLO) is unique among the structurally, characterized copper amine oxidases in being able to oxidize the side, chain of lysine residues in polypeptides. Remarkably, the yeast PPLO is, nearly as effective in oxidizing a mammalian tropoelastin substrate as is, a true mammalian lysyl oxidase isolated from bovine aorta. Thus, PPLO is, functionally related to the copper-containing lysyl oxidases despite the, lack of any significant sequence similarity with these enzymes. The, structure of PPLO has been determined at 1.65 A resolution. PPLO is a, homodimer in which each subunit contains a Type II copper atom and a, topaquinone cofactor (TPQ) formed by the posttranslational modification of, a tyrosine residue. While PPLO has tertiary and quaternary topologies, similar to those found in other quinone-containing copper amine oxidases, its active site is substantially more exposed and accessible. The, structural elements that are responsible for the accessibility of the, active site are identified and discussed.

About this Structure

1N9E is a Single protein structure of sequence from Pichia pastoris with NAG, CU, CA and SO4 as ligands. Active as Protein-lysine 6-oxidase, with EC number 1.4.3.13 Full crystallographic information is available from OCA.

Reference

The crystal structure of Pichia pastoris lysyl oxidase., Duff AP, Cohen AE, Ellis PJ, Kuchar JA, Langley DB, Shepard EM, Dooley DM, Freeman HC, Guss JM, Biochemistry. 2003 Dec 30;42(51):15148-57. PMID:14690425

Page seeded by OCA on Sat Nov 24 22:46:12 2007