1so9

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Solution Structure of apoCox11, 30 structures

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

1SO9 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

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