==PSAO and Xenon==

<StructureSection load='1w2z' size='340' side='right'caption='[[1w2z]], [[Resolution|resolution]] 2.24&Aring;' scene=''>

<table><tr><td colspan='2'>[[1w2z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W2Z FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2z OCA], [http://pdbe.org/1w2z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w2z RCSB], [http://www.ebi.ac.uk/pdbsum/1w2z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w2z ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:15533431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1w2z" style="background-color:#fffaf0;"></div>

==See Also==

*[[Copper Amine Oxidase|Copper Amine Oxidase]]

== References ==

<references/>

[[Category: Oxidoreductase]]

[[Category: Metal-binding oxidase]]

[[Category: Xenon]]