2ic0
From Proteopedia
(New page: 200px<br /><applet load="2ic0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ic0, resolution 1.780Å" /> '''Urate oxidase under...) |
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| - | [[Image:2ic0.jpg|left|200px]]<br /><applet load="2ic0" size=" | + | [[Image:2ic0.jpg|left|200px]]<br /><applet load="2ic0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ic0, resolution 1.780Å" /> | caption="2ic0, resolution 1.780Å" /> | ||
'''Urate oxidase under 2.0 MPa pressure of xenon'''<br /> | '''Urate oxidase under 2.0 MPa pressure of xenon'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In contrast with most inhalational anesthetics, the anesthetic gases xenon | + | In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia. |
==About this Structure== | ==About this Structure== | ||
| - | 2IC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with NA, ACE, AZA and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http:// | + | 2IC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=AZA:'>AZA</scene> and <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IC0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Urate oxidase]] | [[Category: Urate oxidase]] | ||
| - | [[Category: Abraini, J | + | [[Category: Abraini, J H.]] |
[[Category: Prange, T.]] | [[Category: Prange, T.]] | ||
[[Category: Retailleau, P.]] | [[Category: Retailleau, P.]] | ||
| - | [[Category: Santos, J | + | [[Category: Santos, J Sopkova-de Oliveira.]] |
| - | [[Category: h, N | + | [[Category: h, N Colloc.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: AZA]] | [[Category: AZA]] | ||
| Line 27: | Line 27: | ||
[[Category: uric acid degradation]] | [[Category: uric acid degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:01 2008'' |
Revision as of 15:51, 21 February 2008
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Urate oxidase under 2.0 MPa pressure of xenon
Overview
In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia.
About this Structure
2IC0 is a Single protein structure of sequence from Aspergillus flavus with , , and as ligands. Active as Urate oxidase, with EC number 1.7.3.3 Full crystallographic information is available from OCA.
Reference
Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action., Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH, Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130
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