1w2z

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spinqualitylabelsall models 1w2z, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PSAO AND XENON

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 ... [(full description)]

About this Structure

1W2Z is a [Single protein] structure of sequence from [Pisum sativum] with NAG, MN, IOD, CU and XE as [ligands]. Active as [[1]], with EC number [1.4.3.6]. 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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