1SP0

Solution Structure of apoCox11

Summary for 1SP0

• Entry DOI: 10.2210/pdb1sp0/pdb
• NMR Information: BMRB: 6190
• Descriptor: Cytochrome C oxidase assembly protein ctaG (1 entity in total)
• Functional Keywords: immunoglobulin-like fold, copper protein, cytochrome c oxidase assembly, metal transport
• Biological source: Sinorhizobium meliloti
• Cellular location: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side (Potential): Q92RG6
• Total number of polymer chains: 1
• Total formula weight: 18388.09

Authors

Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S.,Gonnelli, L.,Mangani, S. (deposition date: 2004-03-16, release date: 2004-08-10, Last modification date: 2024-05-22)

Primary citation

Banci, L.,Bertini, I.,Cantini, F.,Ciofi-Baffoni, S.,Gonnelli, L.,Mangani, S.
Solution Structure of Cox11, a Novel Type of {beta}-Immunoglobulin-like Fold Involved in CuB Site Formation of Cytochrome c Oxidase.
J.Biol.Chem., 279:34833-34839, 2004

PubMed Abstract: 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.

PubMed: 15181013
DOI: 10.1074/jbc.M403655200

Experimental method

SOLUTION NMR