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< | ==Solution structure of apo-DR1885 from Deinococcus radiodurans== | ||
<StructureSection load='2jqa' size='340' side='right'caption='[[2jqa]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1x7l 1x7l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQA FirstGlance]. <br> | |||
</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'>[https://proteopedia.org/fgij/fg.htm?mol=2jqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqa OCA], [https://pdbe.org/2jqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqa RCSB], [https://www.ebi.ac.uk/pdbsum/2jqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqa ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RT80_DEIRA Q9RT80_DEIRA] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/2jqa_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jqa ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sco1 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<ref>PMID:15753304</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jqa" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Deinococcus radiodurans R1]] | |||
[[Category: Large Structures]] | |||
[[Category: Banci L]] | |||
== | [[Category: Bertini I]] | ||
[[Category: Ciofi Baffoni S]] | |||
[[Category: Deinococcus radiodurans]] | [[Category: Katsari E]] | ||
[[Category: | [[Category: Katsaros N]] | ||
[[Category: | [[Category: Kubicek K]] | ||
[[Category: | |||
[[Category: | |||
[[Category: Katsari | |||
[[Category: Katsaros | |||
[[Category: Kubicek | |||
Latest revision as of 13:10, 20 December 2023
Solution structure of apo-DR1885 from Deinococcus radioduransSolution structure of apo-DR1885 from Deinococcus radiodurans
Structural highlights
FunctionEvolutionary 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. References |
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