1z2g
From Proteopedia
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| - | [[Image:1z2g.gif|left|200px]] | + | [[Image:1z2g.gif|left|200px]] |
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| - | '''Solution structure of apo, oxidized yeast Cox17''' | + | {{Structure |
| + | |PDB= 1z2g |SIZE=350|CAPTION= <scene name='initialview01'>1z2g</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= YLL009C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of apo, oxidized yeast Cox17''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z2G is a [ | + | 1Z2G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2G OCA]. |
==Reference== | ==Reference== | ||
| - | Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding., Arnesano F, Balatri E, Banci L, Bertini I, Winge DR, Structure. 2005 May;13(5):713-22. PMID:[http:// | + | Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding., Arnesano F, Balatri E, Banci L, Bertini I, Winge DR, Structure. 2005 May;13(5):713-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15893662 15893662] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: copper chaperone]] | [[Category: copper chaperone]] | ||
[[Category: cytochrome c oxidase assembly]] | [[Category: cytochrome c oxidase assembly]] | ||
| - | [[Category: disulfide | + | [[Category: disulfide bond]] |
[[Category: spine]] | [[Category: spine]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:26 2008'' |
Revision as of 13:30, 20 March 2008
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| Gene: | YLL009C (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of apo, oxidized yeast Cox17
Overview
Cox17 is a key mitochondrial copper chaperone involved in the assembly of cytochrome c oxidase (COX). The NMR solution structure of the oxidized apoCox17 isoform consists of a coiled-coil conformation stabilized by two disulfide bonds involving Cys(26)/Cys(57) and Cys(36)/Cys(47). This appears to be a conserved tertiary fold of a class of proteins, localized within the mitochondrial intermembrane space, that contain a twin Cys-x(9)-Cys sequence motif. An isomerization of one disulfide bond from Cys(26)/Cys(57) to Cys(24)/Cys(57) is required prior to Cu(I) binding to form the Cu(1)Cox17 complex. Upon further oxidation of the apo-protein, a form with three disulfide bonds is obtained. The reduction of all disulfide bonds provides a molten globule form that can convert to an additional conformer capable of binding up to four Cu(I) ions in a polycopper cluster. This form of the protein is oligomeric. These properties are framed within a complete model of mitochondrial import and COX assembly.
About this Structure
1Z2G is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding., Arnesano F, Balatri E, Banci L, Bertini I, Winge DR, Structure. 2005 May;13(5):713-22. PMID:15893662
Page seeded by OCA on Thu Mar 20 15:30:26 2008
Categories: Saccharomyces cerevisiae | Single protein | Arnesano, F. | Balatri, E. | Banci, L. | Bertini, I. | SPINE, Structural Proteomics in Europe. | Winge, D R. | Coiled coil-helix-coiled coil-helix domain | Copper chaperone | Cytochrome c oxidase assembly | Disulfide bond | Spine | Structural genomic | Structural proteomics in europe
