1to5
From Proteopedia
(New page: 200px<br /><applet load="1to5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1to5, resolution 2.20Å" /> '''Structure of the cyt...) |
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| - | [[Image:1to5.jpg|left|200px]]<br /><applet load="1to5" size=" | + | [[Image:1to5.jpg|left|200px]]<br /><applet load="1to5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1to5, resolution 2.20Å" /> | caption="1to5, resolution 2.20Å" /> | ||
'''Structure of the cytosolic Cu,Zn SOD from S. mansoni'''<br /> | '''Structure of the cytosolic Cu,Zn SOD from S. mansoni'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cu,Zn superoxide dismutase (Cu,Zn SOD) is an essential enzyme for | + | Cu,Zn superoxide dismutase (Cu,Zn SOD) is an essential enzyme for protecting cells from the toxic effects of reactive oxygen species. In humans, two distinct Cu,Zn SOD genes are located on chromosomes 4 and 21 and mutations in the latter have been associated with familial amyotrophic lateral sclerosis. Similarly, schistosomes (trematode parasites responsible for the chronically debilitating disease schistosomiasis) also produce two distinct Cu,Zn SODs, in this case one cytosolic and one bearing a signal peptide. The crystal structure of the cytosolic form of the enzyme from the human trematode Schistosoma mansoni (SmCtSOD) was solved and refined to a resolution of 2.2 A (space group P2(1)2(1)2(1), R = 17.6% and R(free) = 24.1%) and 1.55 A (space group P2(1), R = 15.7% and R(free) = 17.1%). This is the first report of a crystal structure of a Cu,Zn superoxide dismutase derived from a human parasite. Alternate positions for the catalytic copper and its water ligand were refined for the 1.55 A SmCtSOD model, but the most interesting structural differences between SmCtSOD and the human homologue reside in the loops used for electrostatic guidance of the substrate to the enzyme active site. |
==About this Structure== | ==About this Structure== | ||
| - | 1TO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni] with ZN, CU and ACT 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:// | + | 1TO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=ACT:'>ACT</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=1TO5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
| - | [[Category: Araujo, A | + | [[Category: Araujo, A P.Ulian de.]] |
| - | [[Category: Cardoso, R | + | [[Category: Cardoso, R M.F.]] |
| - | [[Category: Garratt, R | + | [[Category: Garratt, R C.]] |
| - | [[Category: Silva, C | + | [[Category: Silva, C H.T P.]] |
[[Category: Tanaka, M.]] | [[Category: Tanaka, M.]] | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
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[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:38 2008'' |
Revision as of 13:15, 21 February 2008
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Structure of the cytosolic Cu,Zn SOD from S. mansoni
Overview
Cu,Zn superoxide dismutase (Cu,Zn SOD) is an essential enzyme for protecting cells from the toxic effects of reactive oxygen species. In humans, two distinct Cu,Zn SOD genes are located on chromosomes 4 and 21 and mutations in the latter have been associated with familial amyotrophic lateral sclerosis. Similarly, schistosomes (trematode parasites responsible for the chronically debilitating disease schistosomiasis) also produce two distinct Cu,Zn SODs, in this case one cytosolic and one bearing a signal peptide. The crystal structure of the cytosolic form of the enzyme from the human trematode Schistosoma mansoni (SmCtSOD) was solved and refined to a resolution of 2.2 A (space group P2(1)2(1)2(1), R = 17.6% and R(free) = 24.1%) and 1.55 A (space group P2(1), R = 15.7% and R(free) = 17.1%). This is the first report of a crystal structure of a Cu,Zn superoxide dismutase derived from a human parasite. Alternate positions for the catalytic copper and its water ligand were refined for the 1.55 A SmCtSOD model, but the most interesting structural differences between SmCtSOD and the human homologue reside in the loops used for electrostatic guidance of the substrate to the enzyme active site.
About this Structure
1TO5 is a Single protein structure of sequence from Schistosoma mansoni with , and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni., Cardoso RM, Silva CH, Ulian de Araujo AP, Tanaka T, Tanaka M, Garratt RC, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1569-78. Epub 2004, Aug 26. PMID:15333927
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