2odx

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|PDB= 2odx |SIZE=350|CAPTION= <scene name='initialview01'>2odx</scene>
|PDB= 2odx |SIZE=350|CAPTION= <scene name='initialview01'>2odx</scene>
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span>
|GENE= COX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= COX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2odx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odx OCA], [http://www.ebi.ac.uk/pdbsum/2odx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2odx RCSB]</span>
}}
}}
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[[Category: Ciofi-Baffoni, S.]]
[[Category: Ciofi-Baffoni, S.]]
[[Category: III, J H.Coyne.]]
[[Category: III, J H.Coyne.]]
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[[Category: ZN]]
 
[[Category: all beta-protein]]
[[Category: all beta-protein]]
[[Category: metallo-protein]]
[[Category: metallo-protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:58:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:16:21 2008''

Revision as of 01:16, 31 March 2008


PDB ID 2odx

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Ligands:
Gene: COX4 (Saccharomyces cerevisiae)
Activity: Cytochrome-c oxidase, with EC number 1.9.3.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Solution structure of Zn(II)Cox4


Overview

Yeast Cox4 is a zinc binding subunit of cytochrome c oxidase. Cox4 is the only cofactor-containing subunit that is not directly part of the catalytic core of the enzyme located in the mitochondrial inner membrane. The Zn(II) site is shown to be distinct from the bovine ortholog, as it results from the x-ray structure of the entire cytochrome c oxidase in having a single histidyl residue and three conserved cysteines residues in the coordination sphere. Substitutions at the Cys ligand positions result in non-functional Cox4 proteins that fail to lead to cytochrome oxidase assembly. Limited function exists in His-119 mutants when overexpressed. Zn(II) binding in Cox4 is, therefore, important for the stability of the complex. The solution structure of yeast Cox4 elucidated by multidimensional NMR reveals a C-terminal globular domain consisting of two beta sheets analogous to the bovine ortholog except the loop containing the coordinating His in the yeast protein and the fourth Cys in the bovine protein are in different positions in the two structures. The conformation of this loop is dictated by the different sequence position of the fourth coordinating zinc ligand. The Zn(II) ion is buried within the domain, consistent with its role in structural stability. Potential functions of this matrix-facing subunit are discussed.

About this Structure

2ODX is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The characterization and role of zinc binding in yeast Cox4., Coyne HJ 3rd, Ciofi-Baffoni S, Banci L, Bertini I, Zhang L, George GN, Winge DR, J Biol Chem. 2007 Mar 23;282(12):8926-34. Epub 2007 Jan 10. PMID:17215247

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