1jk9

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(New page: 200px<br /><applet load="1jk9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jk9, resolution 2.9&Aring;" /> '''Heterodimer between H...)
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[[Image:1jk9.jpg|left|200px]]<br /><applet load="1jk9" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jk9.jpg|left|200px]]<br /><applet load="1jk9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jk9, resolution 2.9&Aring;" />
caption="1jk9, resolution 2.9&Aring;" />
'''Heterodimer between H48F-ySOD1 and yCCS'''<br />
'''Heterodimer between H48F-ySOD1 and yCCS'''<br />
==Overview==
==Overview==
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The copper chaperone for superoxide dismutase (CCS) activates the, eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1)., The 2.9 A resolution structure of yeast SOD1 complexed with yeast CCS, (yCCS) reveals that SOD1 interacts with its metallochaperone to form a, complex comprising one monomer of each protein. The heterodimer interface, is remarkably similar to the SOD1 and yCCS homodimer interfaces. Striking, conformational rearrangements are observed in both the chaperone and, target enzyme upon complex formation, and the functionally essential, C-terminal domain of yCCS is well positioned to play a key role in the, metal ion transfer mechanism. This domain is linked to SOD1 by an, intermolecular disulfide bond that may facilitate or regulate copper, delivery.
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The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 A resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD1 interacts with its metallochaperone to form a complex comprising one monomer of each protein. The heterodimer interface is remarkably similar to the SOD1 and yCCS homodimer interfaces. Striking conformational rearrangements are observed in both the chaperone and target enzyme upon complex formation, and the functionally essential C-terminal domain of yCCS is well positioned to play a key role in the metal ion transfer mechanism. This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery.
==About this Structure==
==About this Structure==
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1JK9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN 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=1JK9 OCA].
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1JK9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</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=1JK9 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
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[[Category: Halloran, T.V.O.]]
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[[Category: Halloran, T V.O.]]
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[[Category: Lamb, A.L.]]
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[[Category: Lamb, A L.]]
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[[Category: Rosenzweig, A.C.]]
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[[Category: Rosenzweig, A C.]]
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[[Category: Torres, A.S.]]
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[[Category: Torres, A S.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:20:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:39 2008''

Revision as of 11:23, 21 February 2008


1jk9, resolution 2.9Å

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Heterodimer between H48F-ySOD1 and yCCS

Overview

The copper chaperone for superoxide dismutase (CCS) activates the eukaryotic antioxidant enzyme copper, zinc superoxide dismutase (SOD1). The 2.9 A resolution structure of yeast SOD1 complexed with yeast CCS (yCCS) reveals that SOD1 interacts with its metallochaperone to form a complex comprising one monomer of each protein. The heterodimer interface is remarkably similar to the SOD1 and yCCS homodimer interfaces. Striking conformational rearrangements are observed in both the chaperone and target enzyme upon complex formation, and the functionally essential C-terminal domain of yCCS is well positioned to play a key role in the metal ion transfer mechanism. This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery.

About this Structure

1JK9 is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.

Reference

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone., Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC, Nat Struct Biol. 2001 Sep;8(9):751-5. PMID:11524675

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