2b7j

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[[Image:2b7j.gif|left|200px]]
[[Image:2b7j.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2b7j |SIZE=350|CAPTION= <scene name='initialview01'>2b7j</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_2b7j", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= SCO1 ([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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{{STRUCTURE_2b7j| PDB=2b7j | SCENE= }}
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|RELATEDENTRY=[[2b7k|2B7K]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7j OCA], [http://www.ebi.ac.uk/pdbsum/2b7j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b7j RCSB]</span>
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'''Crystal Structure of Yeast Sco1 with Copper Bound'''
'''Crystal Structure of Yeast Sco1 with Copper Bound'''
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[[Category: Abajian, C.]]
[[Category: Abajian, C.]]
[[Category: Rosenzweig, A C.]]
[[Category: Rosenzweig, A C.]]
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[[Category: cytochrome c oxidase]]
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[[Category: Cytochrome c oxidase]]
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[[Category: metallochaperone]]
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[[Category: Metallochaperone]]
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[[Category: sco]]
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[[Category: Sco]]
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[[Category: sco1]]
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[[Category: Sco1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:57:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:29 2008''
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Revision as of 16:57, 3 May 2008

Image:2b7j.gif

Template:STRUCTURE 2b7j

Crystal Structure of Yeast Sco1 with Copper Bound


Overview

The Sco family of proteins are involved in the assembly of the dinuclear CuA site in cytochrome c oxidase (COX), the terminal enzyme in aerobic respiration. These proteins, which are found in both eukaryotes and prokaryotes, are characterized by a conserved CXXXC sequence motif that binds copper ions and that has also been proposed to perform a thiol:disulfide oxidoreductase function. The crystal structures of Saccharomyces cerevisiae apo Sco1 (apo-ySco1) and Sco1 in the presence of copper ions (Cu-ySco1) were determined to 1.8- and 2.3-A resolutions, respectively. Yeast Sco1 exhibits a thioredoxin-like fold, similar to that observed for human Sco1 and a homolog from Bacillus subtilis. The Cu-ySco1 structure, obtained by soaking apo-ySco1 crystals in copper ions, reveals an unexpected copper-binding site involving Cys181 and Cys216, cysteine residues present in ySco1 but not in other homologs. The conserved CXXXC cysteines, Cys148 and Cys152, can undergo redox chemistry in the crystal. An essential histidine residue, His239, is located on a highly flexible loop, denoted the Sco loop, and can adopt positions proximal to both pairs of cysteines. Interactions between ySco1 and its partner proteins yeast Cox17 and yeast COX2 are likely to occur via complementary electrostatic surfaces. This high-resolution model of a eukaryotic Sco protein provides new insight into Sco copper binding and function.

About this Structure

2B7J is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of yeast Sco1., Abajian C, Rosenzweig AC, J Biol Inorg Chem. 2006 Jun;11(4):459-66. Epub 2006 Mar 29. PMID:16570183 Page seeded by OCA on Sat May 3 19:57:09 2008

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