This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2jqa

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution structure of apo-DR1885 from Deinococcus radiodurans

Structural highlights

2jqa is a 1 chain structure with sequence from Deinococcus radiodurans R1. This structure supersedes the now removed PDB entry 1x7l. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9RT80_DEIRA

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Banci L, Bertini I, Ciofi-Baffoni S, Katsari E, Katsaros N, Kubicek K, Mangani S. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase. Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3994-9. Epub 2005 Mar 7. PMID:15753304

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jqa"

@@ Line 1: / Line 1: @@
 ==Solution structure of apo-DR1885 from Deinococcus radiodurans==
-<StructureSection load='2jqa' size='340' side='right'caption='[[2jqa]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2jqa' size='340' side='right'caption='[[2jqa]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deira Deira]. 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>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x9l|1x9l]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DR1885 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 DEIRA])</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]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Deira]]
+[[Category: Deinococcus radiodurans R1]]
 [[Category: Large Structures]]
-[[Category: Baffoni, S Ciofi]]
+[[Category: Banci L]]
-[[Category: Banci, L]]
+[[Category: Bertini I]]
-[[Category: Bertini, I]]
+[[Category: Ciofi Baffoni S]]
-[[Category: Katsari, E]]
+[[Category: Katsari E]]
-[[Category: Katsaros, N]]
+[[Category: Katsaros N]]
-[[Category: Kubicek, K]]
+[[Category: Kubicek K]]
-[[Category: Copper binding protein]]
-[[Category: Metal binding protein]]

2jqa

From Proteopedia

Current revision

Solution structure of apo-DR1885 from Deinococcus radiodurans

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox