1rky
From Proteopedia
(New page: 200px<br /><applet load="1rky" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rky, resolution 1.68Å" /> '''PPLO + Xe'''<br /> ...) |
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| - | [[Image:1rky.gif|left|200px]]<br /><applet load="1rky" size=" | + | [[Image:1rky.gif|left|200px]]<br /><applet load="1rky" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rky, resolution 1.68Å" /> | caption="1rky, resolution 1.68Å" /> | ||
'''PPLO + Xe'''<br /> | '''PPLO + Xe'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Potential dioxygen-binding sites in three Cu amine oxidases have been | + | 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== | ||
| - | 1RKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with NAG, CU, CA, MG, CL, IMD and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] Full crystallographic information is available from [http:// | + | 1RKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=IMD:'>IMD</scene> and <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-lysine 6-oxidase]] | [[Category: Protein-lysine 6-oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Duff, A | + | [[Category: Duff, A P.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: xenon]] | [[Category: xenon]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:00 2008'' |
Revision as of 12:52, 21 February 2008
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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 , , , , , and 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
Page seeded by OCA on Thu Feb 21 14:52:00 2008
Categories: Pichia pastoris | Protein-lysine 6-oxidase | Single protein | Duff, A P. | Guss, J M. | CA | CL | CU | IMD | MG | NAG | XE | Amine oxidase | Cao | Copper-containing | Cuao | Dioxygen binding site | Lysyl oxidase | Oxygen binding site | Pplo | Quinone | Tpq | Trihydroxyphenylalanine quinone | Xenon
