1qup
From Proteopedia
(New page: 200px<br /><applet load="1qup" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qup, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1qup.jpg|left|200px]]<br /><applet load="1qup" size=" | + | [[Image:1qup.jpg|left|200px]]<br /><applet load="1qup" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qup, resolution 1.80Å" /> | caption="1qup, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE'''<br /> | '''CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific | + | Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 A resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone. |
==About this Structure== | ==About this Structure== | ||
| - | 1QUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Halloran, T | + | [[Category: Halloran, T V.O.]] |
| - | [[Category: Lamb, A | + | [[Category: Lamb, A L.]] |
| - | [[Category: Pufahl, R | + | [[Category: Pufahl, R A.]] |
| - | [[Category: Rosenzweig, A | + | [[Category: Rosenzweig, A C.]] |
| - | [[Category: Wernimont, A | + | [[Category: Wernimont, A K.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: beta-alpha-beta-beta-alpha-beta and beta barrel]] | [[Category: beta-alpha-beta-beta-alpha-beta and beta barrel]] | ||
[[Category: two domains]] | [[Category: two domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:59 2008'' |
Revision as of 12:44, 21 February 2008
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CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE
Overview
Cellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 A resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone.
About this Structure
1QUP is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the copper chaperone for superoxide dismutase., Lamb AL, Wernimont AK, Pufahl RA, Culotta VC, O'Halloran TV, Rosenzweig AC, Nat Struct Biol. 1999 Aug;6(8):724-9. PMID:10426947
Page seeded by OCA on Thu Feb 21 14:43:59 2008
