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| | ==Solution structure of apoCopC from Pseudomonas syringae== | | ==Solution structure of apoCopC from Pseudomonas syringae== |
| - | <StructureSection load='1m42' size='340' side='right'caption='[[1m42]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1m42' size='340' side='right'caption='[[1m42]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1m42]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M42 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1m42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M42 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COPC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m42 OCA], [http://pdbe.org/1m42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m42 RCSB], [http://www.ebi.ac.uk/pdbsum/1m42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m42 ProSAT]</span></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=1m42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m42 OCA], [https://pdbe.org/1m42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m42 RCSB], [https://www.ebi.ac.uk/pdbsum/1m42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m42 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COPC_PSEUB COPC_PSEUB]] Mediates copper resistance by sequestration of copper in the periplasm along with the copper-binding protein CopA. | + | [https://www.uniprot.org/uniprot/Q4ZWC7_PSEU2 Q4ZWC7_PSEU2] Involved in copper resistance.[RuleBase:RU369037] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 19310]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arnesano, F]] | + | [[Category: Pseudomonas syringae]] |
| - | [[Category: Banci, L]] | + | [[Category: Arnesano F]] |
| - | [[Category: Bertini, I]] | + | [[Category: Banci L]] |
| - | [[Category: Thompsett, A R]] | + | [[Category: Bertini I]] |
| - | [[Category: Copper trafficking]]
| + | [[Category: Thompsett AR]] |
| - | [[Category: Cupredoxin]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
Q4ZWC7_PSEU2 Involved in copper resistance.[RuleBase:RU369037]
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
The structure of the metal-free form of CopC, a protein involved in copper homeostasis, has been obtained. The fold is a Greek key beta barrel similar to that of functionally unrelated blue copper proteins but with important structural variations. The protein binds one equivalent of copper (II) with relatively high affinity and contains a cluster of conserved residues (His1, Glu27, Asp89, and His91) which could form a water-accessible metal binding site. The structure also reveals a loop containing the M(X)(n)M motif which is present in a number of proteins also involved in copper homeostasis. The present structure represents a link between copper-trafficking proteins and cupredoxins. Within a structural and genomic analysis, the role of CopC in copper trafficking is discussed.
Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis.,Arnesano F, Banci L, Bertini I, Thompsett AR Structure. 2002 Oct;10(10):1337-47. PMID:12377120[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arnesano F, Banci L, Bertini I, Thompsett AR. Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis. Structure. 2002 Oct;10(10):1337-47. PMID:12377120
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