1rjo: Difference between revisions

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[[Image:1rjo.gif|left|200px]]
{{Seed}}
[[Image:1rjo.png|left|200px]]


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{{STRUCTURE_1rjo|  PDB=1rjo  |  SCENE=  }}  
{{STRUCTURE_1rjo|  PDB=1rjo  |  SCENE=  }}  


'''AGAO + Xe'''
===AGAO + Xe===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_15533431}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15533431}}


==About this Structure==
==About this Structure==
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[[Category: Trihydroxyphenylalanine quinone]]
[[Category: Trihydroxyphenylalanine quinone]]
[[Category: Xenon]]
[[Category: Xenon]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:34:45 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:38:59 2008''

Revision as of 09:39, 29 July 2008

File:1rjo.png

Template:STRUCTURE 1rjo

AGAO + Xe

Template:ABSTRACT PUBMED 15533431

About this Structure

1RJO is a Single protein structure of sequence from Arthrobacter globiformis. 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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