1rky

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spinqualitylabelsall models 1rky, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PPLO + Xe

Overview

Potential dioxygen-binding sites in three Cu amine oxidases have been, investigated by recording X-ray diffraction data at 1.7-2.2A resolution, for crystals under a high pressure of xenon gas. Electron-density, difference maps and crystallographic refinement provide unequivocal, evidence for a number of Xe-binding sites in each enzyme. Only one of, these sites is present in all three Cu amine oxidases studied. Structural, changes elsewhere in the protein molecules are insignificant. The results, illustrate the use of xenon as a probe for cavities, in which a protein, may accommodate a dioxygen molecule. The finding of a potential, dioxygen-binding cavity close to the active site of Cu amine oxidases may, be relevant to the function of the enzymes, since the formation of a, transient protein-dioxygen complex is a likely step in the catalytic, mechanism. No evidence was found for xenon binding in a region of the, molecule that was previously identified in two other Cu amine oxidases as, a potential transient dioxygen-binding site.

About this Structure

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

Reference

Using xenon as a probe for dioxygen-binding sites in copper amine oxidases., Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM, J Mol Biol. 2004 Nov 26;344(3):599-607. PMID:15533431

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