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| | ==Solution Structure of apoCox11== | | ==Solution Structure of apoCox11== |
| - | <StructureSection load='1sp0' size='340' side='right'caption='[[1sp0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1sp0' size='340' side='right'caption='[[1sp0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sp0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_9930 Atcc 9930]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SP0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sp0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SP0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTAG, R00908, SMC00012 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 ATCC 9930])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp0 OCA], [http://pdbe.org/1sp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sp0 RCSB], [http://www.ebi.ac.uk/pdbsum/1sp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp0 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp0 OCA], [https://pdbe.org/1sp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp0 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COXZ_RHIME COXZ_RHIME]] Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I (By similarity). | + | [https://www.uniprot.org/uniprot/COXZ_RHIME COXZ_RHIME] Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 9930]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Sinorhizobium meliloti]] |
| - | [[Category: Bertini, I]] | + | [[Category: Banci L]] |
| - | [[Category: Cantini, F]] | + | [[Category: Bertini I]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Cantini F]] |
| - | [[Category: Gonnelli, L]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: Mangani, S]] | + | [[Category: Gonnelli L]] |
| - | [[Category: Copper protein]]
| + | [[Category: Mangani S]] |
| - | [[Category: Cytochrome c oxidase assembly]]
| + | |
| - | [[Category: Immunoglobulin-like fold]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| Structural highlights
Function
COXZ_RHIME Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2004 Aug 13;279(33):34833-9. Epub 2004 Jun 4. PMID:15181013 doi:http://dx.doi.org/10.1074/jbc.M403655200
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