1sda
From Proteopedia
(New page: 200px<br /><applet load="1sda" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sda, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1sda.gif|left|200px]]<br /><applet load="1sda" size=" | + | [[Image:1sda.gif|left|200px]]<br /><applet load="1sda" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sda, resolution 2.5Å" /> | caption="1sda, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE'''<br /> | '''CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of bovine Cu,Zn superoxide dismutase modified with | + | The crystal structure of bovine Cu,Zn superoxide dismutase modified with peroxynitrite (ONOO-) was determined by X-ray diffraction, utilizing the existing three-dimensional model of the native structure deposited in the Brookhaven Protein Data Bank (J. A. Tainer et al., J. Mol. Biol. 160, 181-217, 1982). The native structure and the modified derivative were refined to R factors of 19.0 and 18.7% respectively using diffraction data from 6.0 to 2.5 A. The major result after reaction with peroxynitrite was the appearance of electron density 1.45 A from a single epsilon carbon of Tyr-108, the only tyrosine residue in the sequence. Tyr-108 is a solvent-exposed residue 18 A from the copper atom in the active site. The electron density was consistent with nitration of Tyr-108 at one of the epsilon carbons to form 3-nitrotyrosine. We propose that the nitration occurs in solution by transfer of a nitronium-like species from the active site on one superoxide dismutase dimer to the Tyr-108 of a second dimer. |
==About this Structure== | ==About this Structure== | ||
| - | 1SDA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NO2, CU, ZN and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http:// | + | 1SDA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NO2:'>NO2</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
| - | [[Category: Beckman, J | + | [[Category: Beckman, J S.]] |
[[Category: Carson, M.]] | [[Category: Carson, M.]] | ||
[[Category: Chen, J.]] | [[Category: Chen, J.]] | ||
[[Category: Ischiropoulos, H.]] | [[Category: Ischiropoulos, H.]] | ||
| - | [[Category: Smith, C | + | [[Category: Smith, C D.]] |
| - | [[Category: Woerd, M | + | [[Category: Woerd, M Van Der.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: oxidoreductase(copper)]] | [[Category: oxidoreductase(copper)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:19 2008'' |
Revision as of 13:00, 21 February 2008
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CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE
Overview
The crystal structure of bovine Cu,Zn superoxide dismutase modified with peroxynitrite (ONOO-) was determined by X-ray diffraction, utilizing the existing three-dimensional model of the native structure deposited in the Brookhaven Protein Data Bank (J. A. Tainer et al., J. Mol. Biol. 160, 181-217, 1982). The native structure and the modified derivative were refined to R factors of 19.0 and 18.7% respectively using diffraction data from 6.0 to 2.5 A. The major result after reaction with peroxynitrite was the appearance of electron density 1.45 A from a single epsilon carbon of Tyr-108, the only tyrosine residue in the sequence. Tyr-108 is a solvent-exposed residue 18 A from the copper atom in the active site. The electron density was consistent with nitration of Tyr-108 at one of the epsilon carbons to form 3-nitrotyrosine. We propose that the nitration occurs in solution by transfer of a nitronium-like species from the active site on one superoxide dismutase dimer to the Tyr-108 of a second dimer.
About this Structure
1SDA is a Single protein structure of sequence from Bos taurus with , , and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase., Smith CD, Carson M, van der Woerd M, Chen J, Ischiropoulos H, Beckman JS, Arch Biochem Biophys. 1992 Dec;299(2):350-5. PMID:1444476
Page seeded by OCA on Thu Feb 21 15:00:19 2008
Categories: Bos taurus | Single protein | Superoxide dismutase | Beckman, J S. | Carson, M. | Chen, J. | Ischiropoulos, H. | Smith, C D. | Woerd, M Van Der. | ACE | CU | NO2 | ZN | Oxidoreductase(copper)
