1q0g: Difference between revisions

Revision as of 15:34, 21 February 2008

Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after full x-ray-induced reduction

OverviewOverview

Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.

About this StructureAbout this Structure

1Q0G is a Single protein structure of sequence from Streptomyces seoulensis 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 nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586

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-[[Image:1q0g.gif|left|200px]]<br /><applet load="1q0g" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q0g.gif|left|200px]]<br /><applet load="1q0g" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q0g, resolution 1.60&Aring;" />
 '''Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after full x-ray-induced reduction'''<br />
 ==Overview==
-Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that, efficiently catalyze the dismutation of superoxide radical anions to, protect biological molecules from oxidative damage. The crystal structure, of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was, determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme, state. NiSOD is a homohexamer consisting of four-helix-bundle subunits., The catalytic center resides in the N-terminal active-site loop, where a, Ni(III) ion is coordinated by the amino group of His-1, the amide group of, Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of, His-1 as axial ligand that is lost in the chemically reduced state as well, as after x-ray-induced reduction. This structure represents a third class, of SODs concerning the catalytic metal species, subunit structure, and, oligomeric organization. It adds a member to the small number of, Ni-metalloenzymes and contributes with its Ni(III) active site to the, general understanding of Ni-related biochemistry. NiSOD is shown to occur, also in bacteria other than Streptomyces and is predicted to be present in, some cyanobacteria.
+Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.
 ==About this Structure==
-Q0G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis] with NI and SO4 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=1Q0G OCA].
+Q0G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=SO4:'>SO4</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=1Q0G OCA].
 ==Reference==
-Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Carugo KD, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15173586 15173586]
+Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15173586 15173586]
 [[Category: Single protein]]
 [[Category: Streptomyces seoulensis]]
 [[Category: Superoxide dismutase]]
-[[Category: Carugo, K.Djinovic.]]
+[[Category: Carugo, K Djinovic.]]
-[[Category: Kang, S.O.]]
+[[Category: Kang, S O.]]
-[[Category: Lee, J.W.]]
+[[Category: Lee, J W.]]
 [[Category: Wuerges, J.]]
-[[Category: Yim, H.S.]]
+[[Category: Yim, H S.]]
-[[Category: Yim, Y.I.]]
+[[Category: Yim, Y I.]]
 [[Category: NI]]
 [[Category: SO4]]
 [[Category: homohexamer of four-helix bundles]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:16:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:30 2008''