1so9
From Proteopedia
(New page: 200px<br /><applet load="1so9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1so9" /> '''Solution Structure of apoCox11, 30 structure...) |
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| - | [[Image:1so9.gif|left|200px]]<br /><applet load="1so9" size=" | + | [[Image:1so9.gif|left|200px]]<br /><applet load="1so9" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of apoCox11, 30 structures'''<br /> | '''Solution Structure of apoCox11, 30 structures'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome c oxidase assembly process involves many accessory proteins | + | 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== | ==About this Structure== | ||
| - | 1SO9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http:// | + | 1SO9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SO9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gonnelli, L.]] | [[Category: Gonnelli, L.]] | ||
[[Category: Mangani, S.]] | [[Category: Mangani, S.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: copper protein]] | [[Category: copper protein]] | ||
[[Category: cytochrome c oxidase assembly]] | [[Category: cytochrome c oxidase assembly]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:31 2008'' |
Revision as of 13:03, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:03:31 2008
Categories: Single protein | Sinorhizobium meliloti | Banci, L. | Bertini, I. | Cantini, F. | Ciofi-Baffoni, S. | Gonnelli, L. | Mangani, S. | SPINE, Structural Proteomics in Europe. | Copper protein | Cytochrome c oxidase assembly | Immunoglobulin-like fold | Spine | Structural genomics | Structural proteomics in europe
