1so9

<StructureSection load='1so9' size='340' side='right'caption='[[1so9]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1so9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_9930 Atcc 9930]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SO9 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sp0|1sp0]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTAG, R00908, SMC00012 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 ATCC 9930])</td></tr>

[[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).

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== 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<ref>PMID:15181013</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1so9" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 9930]]

[[Category: Banci, L]]

[[Category: Bertini, I]]

[[Category: Cantini, F]]

[[Category: Ciofi-Baffoni, S]]

[[Category: Gonnelli, L]]

[[Category: Mangani, S]]

[[Category: Structural proteomics in europe]]