1sp0
From Proteopedia
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'''Solution Structure of apoCox11''' | '''Solution Structure of apoCox11''' | ||
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[[Category: Gonnelli, L.]] | [[Category: Gonnelli, L.]] | ||
[[Category: Mangani, S.]] | [[Category: Mangani, S.]] | ||
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- | [[Category: | + | [[Category: Cytochrome c oxidase assembly]] |
- | [[Category: | + | [[Category: Immunoglobulin-like fold]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:58:15 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 05:58, 3 May 2008
Solution Structure of apoCox11
Overview
Cytochrome c oxidase assembly process involves many accessory proteins including Cox11, which is a copper-binding protein required for Cu incorporation into the Cu(B) site of cytochrome c oxidase. In a genome wide search, a number of Cox11 homologs are found in all of the eukaryotes with complete genomes and in several Gram-negative bacteria. All of them possess a highly homologous soluble domain and contain an N-terminal fragment that anchors the protein to the membrane. An anchor-free construct of 164 amino acids was obtained from Sinorhizobium meliloti, and the first structure of this class of proteins is reported here. The apoform has an immunoglobulin-like fold with a novel type of beta-strand organization. The copper binding motif composed of two highly conserved cysteines is located on one side of the beta-barrel structure. The apoprotein is monomeric in the presence of dithiothreitol, whereas it dimerizes in the absence of the reductant. When copper(I) binds, NMR and extended x-ray absorption fine structure (EXAFS) data indicate a dimeric protein state with two thiolates bridging two copper(I) ions. The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly.
About this Structure
1SP0 is a Single protein structure of sequence from Sinorhizobium meliloti. Full crystallographic information is available from OCA.
Reference
Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase., Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Gonnelli L, Mangani S, J Biol Chem. 2004 Aug 13;279(33):34833-9. Epub 2004 Jun 4. PMID:15181013 Page seeded by OCA on Sat May 3 08:58:15 2008