1x9l: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1x9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X9L FirstGlance]. <br> | <table><tr><td colspan='2'>[[1x9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X9L FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x9l RCSB], [http://www.ebi.ac.uk/pdbsum/1x9l PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x9l RCSB], [http://www.ebi.ac.uk/pdbsum/1x9l PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Banci, L | [[Category: Banci, L]] | ||
[[Category: Bertini, I | [[Category: Bertini, I]] | ||
[[Category: Ciofi-Baffoni, S | [[Category: Ciofi-Baffoni, S]] | ||
[[Category: Katsari, E | [[Category: Katsari, E]] | ||
[[Category: Katsaros, N | [[Category: Katsaros, N]] | ||
[[Category: Kubicek, K | [[Category: Kubicek, K]] | ||
[[Category: SPINE, Structural Proteomics in Europe | [[Category: SPINE, Structural Proteomics in Europe]] | ||
[[Category: Copper binding protein]] | [[Category: Copper binding protein]] | ||
[[Category: Deinococcus radioduran]] | [[Category: Deinococcus radioduran]] | ||
Revision as of 15:43, 6 January 2015
Solution structure of CuI-DR1885 from Deinococcus RadioduransSolution structure of CuI-DR1885 from Deinococcus Radiodurans
Structural highlights
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 PubMedSco1 and Cox17 are accessory proteins required for the correct assembly of eukaryotic cytochrome c oxidase. At variance with Sco1, Cox17 orthologs are found only in eukaryotes. We browsed bacterial genomes to search proteins functionally equivalent to Cox17, and we identified a class of proteins of unknown function displaying a conserved gene neighborhood to bacterial Sco1 genes, all sharing a potential metal binding motif H(M)X10MX21HXM. Two members of this group, DR1885 from Deinococcus radiodurans and CC3502 from Caulobacter crescentus, were expressed, and their interaction with copper was investigated. The solution structure and extended x-ray absorption fine structure data on the former protein reveal that the protein binds copper(I) through a histidine and three Mets in a cupredoxin-like fold. The surface location of the copper-binding site as well as the type of coordination are well poised for metal transfer chemistry, suggesting that DR1885 might transfer copper, taking the role of Cox17 in bacteria. On the basis of our results, a possible pathway for copper delivery to the Cu(A) center in bacteria is proposed. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.,Banci L, Bertini I, Ciofi-Baffoni S, Katsari E, Katsaros N, Kubicek K, Mangani S Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3994-9. Epub 2005 Mar 7. PMID:15753304[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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