1q0e: Difference between revisions

Revision as of 15:34, 21 February 2008

Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase

OverviewOverview

Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial amyotrophic lateral sclerosis (motor neuron disease). We have determined the structure of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution structure for an intact CuZnSOD and one of only a small number for metalloproteins. For the first time, both subunits have been captured with the three coordinate Cu(I) ligation required by the generally accepted catalytic mechanism, where dismutation of the superoxide radical occurs via reduction of Cu. Furthermore, the improved resolution compared to previous studies (to 1.65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes.

About this StructureAbout this Structure

1Q0E 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

Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A., Hough MA, Hasnain SS, Structure. 2003 Aug;11(8):937-46. PMID:12906825

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OCA

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-[[Image:1q0e.gif|left|200px]]<br /><applet load="1q0e" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q0e.gif|left|200px]]<br /><applet load="1q0e" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q0e, resolution 1.15&Aring;" />
 '''Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase'''<br />
 ==Overview==
-Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of, the cellular response to oxidative stress by catalyzing the dismutation of, the superoxide radical to hydrogen peroxide and water. Mutations in human, CuZnSOD are associated with the development of familial amyotrophic, lateral sclerosis (motor neuron disease). We have determined the structure, of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution, structure for an intact CuZnSOD and one of only a small number for, metalloproteins. For the first time, both subunits have been captured with, the three coordinate Cu(I) ligation required by the generally accepted, catalytic mechanism, where dismutation of the superoxide radical occurs, via reduction of Cu. Furthermore, the improved resolution compared to, previous studies (to 1.65 A) has allowed a more detailed examination of, the metal center environment and its associated water network in the, active site channel, facilitating the analysis of potential proton, transfer routes.
+Copper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial amyotrophic lateral sclerosis (motor neuron disease). We have determined the structure of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution structure for an intact CuZnSOD and one of only a small number for metalloproteins. For the first time, both subunits have been captured with the three coordinate Cu(I) ligation required by the generally accepted catalytic mechanism, where dismutation of the superoxide radical occurs via reduction of Cu. Furthermore, the improved resolution compared to previous studies (to 1.65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes.
 ==About this Structure==
-Q0E 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 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=1Q0E OCA].
+Q0E 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=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=1Q0E OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Superoxide dismutase]]
-[[Category: Hasnain, S.S.]]
+[[Category: Hasnain, S S.]]
-[[Category: Hough, M.A.]]
+[[Category: Hough, M A.]]
 [[Category: ACE]]
 [[Category: CU]]
@@ Line 25: / Line 25: @@
 [[Category: zinc]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:16:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:36 2008''