1w2z: Difference between revisions
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==Overview== | ==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 .. | 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== | ==About this Structure== | ||
1W2Z is a | 1W2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with NAG, MN, IOD, CU and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W2Z OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: xenon]] | [[Category: xenon]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:48:50 2007'' | ||
