1m42: Difference between revisions
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[[Image: | ==Solution structure of apoCopC from Pseudomonas syringae== | ||
<StructureSection load='1m42' size='340' side='right' caption='[[1m42]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1m42]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M42 FirstGlance]. <br> | |||
</td></tr><tr><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 Pseudomonas syringae])</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=1m42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m42 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m42 RCSB], [http://www.ebi.ac.uk/pdbsum/1m42 PDBsum]</span></td></tr> | |||
<table> | |||
== 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/m4/1m42_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:12377120</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Pseudomonas syringae]] | [[Category: Pseudomonas syringae]] | ||
[[Category: Arnesano, F.]] | [[Category: Arnesano, F.]] | ||
Revision as of 17:58, 28 September 2014
Solution structure of apoCopC from Pseudomonas syringaeSolution structure of apoCopC from Pseudomonas syringae
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 PubMedThe 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 |
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