1sda: Difference between revisions

Revision as of 16:00, 21 February 2008

CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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OCA

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-[[Image:1sda.gif|left|200px]]<br /><applet load="1sda" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sda.gif|left|200px]]<br /><applet load="1sda" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sda, resolution 2.5&Aring;" />
 '''CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE'''<br />
 ==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.
+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==
-SDA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SDA OCA].
+SDA 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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Superoxide dismutase]]
-[[Category: Beckman, J.S.]]
+[[Category: Beckman, J S.]]
 [[Category: Carson, M.]]
 [[Category: Chen, J.]]
 [[Category: Ischiropoulos, H.]]
-[[Category: Smith, C.D.]]
+[[Category: Smith, C D.]]
-[[Category: Woerd, M.Van.Der.]]
+[[Category: Woerd, M Van Der.]]
 [[Category: ACE]]
 [[Category: CU]]
@@ Line 26: / Line 26: @@
 [[Category: oxidoreductase(copper)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:17:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:19 2008''