1nm4: Difference between revisions
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==Solution structure of Cu(I)-CopC from Pseudomonas syringae== | |||
<StructureSection load='1nm4' size='340' side='right'caption='[[1nm4]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nm4]] 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=1NM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM4 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=1nm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm4 OCA], [https://pdbe.org/1nm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4ZWC7_PSEU2 Q4ZWC7_PSEU2] Involved in copper resistance.[RuleBase:RU369037] | |||
== 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/nm/1nm4_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=1nm4 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The protein CopC from Pseudomonas syringae has been found capable of binding copper(I) and copper(II) at two different sites, occupied either one at a time or simultaneously. The protein, consisting of 102 amino acids, is known to bind copper(II) in a position that is now found consistent with a coordination arrangement including His-1, Glu-27, Asp-89, and His-91. A full solution structure analysis is reported here for Cu(I)-CopC. The copper(I) site is constituted by His-48 and three of the four Met residues (40, 43, 46, 51), which are clustered in a Met-rich region. Both copper binding sites have been characterized through extended x-ray absorption fine structure studies. They represent novel coordination environments for copper in proteins. The two sites are approximately 30 A far apart and have little affinity for the ion in the other oxidation state. Oxidation of Cu(I)-CopC or reduction of Cu(II)-CopC causes migration of copper from one site to the other. This behavior is observed both in NMR and EXAFS studies and indicates that CopC can exchange copper between two sites activated by a redox switch. CopC resides in the periplasm of Gram-negative bacteria where there is a multicopper oxidase, CopA, which may modulate the redox state of copper. CopC and CopA are coded in the same operon, responsible for copper resistance. These peculiar and novel properties of CopC are discussed with respect to their relevance for copper homeostasis. | |||
A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.,Arnesano F, Banci L, Bertini I, Mangani S, Thompsett AR Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3814-9. Epub 2003 Mar 21. PMID:12651950<ref>PMID:12651950</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nm4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
[[Category: Arnesano | [[Category: Arnesano F]] | ||
[[Category: Banci | [[Category: Banci L]] | ||
[[Category: Bertini | [[Category: Bertini I]] | ||
[[Category: Mangani | [[Category: Mangani S]] | ||
[[Category: Thompsett AR]] | |||
[[Category: Thompsett | |||
Latest revision as of 11:54, 22 May 2024
Solution structure of Cu(I)-CopC from Pseudomonas syringaeSolution structure of Cu(I)-CopC from Pseudomonas syringae
Structural highlights
FunctionQ4ZWC7_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 PubMedThe protein CopC from Pseudomonas syringae has been found capable of binding copper(I) and copper(II) at two different sites, occupied either one at a time or simultaneously. The protein, consisting of 102 amino acids, is known to bind copper(II) in a position that is now found consistent with a coordination arrangement including His-1, Glu-27, Asp-89, and His-91. A full solution structure analysis is reported here for Cu(I)-CopC. The copper(I) site is constituted by His-48 and three of the four Met residues (40, 43, 46, 51), which are clustered in a Met-rich region. Both copper binding sites have been characterized through extended x-ray absorption fine structure studies. They represent novel coordination environments for copper in proteins. The two sites are approximately 30 A far apart and have little affinity for the ion in the other oxidation state. Oxidation of Cu(I)-CopC or reduction of Cu(II)-CopC causes migration of copper from one site to the other. This behavior is observed both in NMR and EXAFS studies and indicates that CopC can exchange copper between two sites activated by a redox switch. CopC resides in the periplasm of Gram-negative bacteria where there is a multicopper oxidase, CopA, which may modulate the redox state of copper. CopC and CopA are coded in the same operon, responsible for copper resistance. These peculiar and novel properties of CopC are discussed with respect to their relevance for copper homeostasis. A redox switch in CopC: an intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites.,Arnesano F, Banci L, Bertini I, Mangani S, Thompsett AR Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3814-9. Epub 2003 Mar 21. PMID:12651950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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