1qup: Difference between revisions

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[[Image:1qup.jpg|left|200px]]
{{Seed}}
[[Image:1qup.png|left|200px]]


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{{STRUCTURE_1qup|  PDB=1qup  |  SCENE=  }}  
{{STRUCTURE_1qup|  PDB=1qup  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE'''
===CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10426947}}


==About this Structure==
==About this Structure==
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[[Category: Beta-alpha-beta-beta-alpha-beta and beta barrel]]
[[Category: Beta-alpha-beta-beta-alpha-beta and beta barrel]]
[[Category: Two domain]]
[[Category: Two domain]]
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