1qup: Difference between revisions
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<StructureSection load='1qup' size='340' side='right'caption='[[1qup]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1qup' size='340' side='right'caption='[[1qup]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qup]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1qup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qup OCA], [https://pdbe.org/1qup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qup RCSB], [https://www.ebi.ac.uk/pdbsum/1qup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qup ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CCS1_YEAST CCS1_YEAST]] Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.<ref>PMID:9295278</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:58, 5 January 2022
CRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASECRYSTAL STRUCTURE OF THE COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE
Structural highlights
Function[CCS1_YEAST] Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.[1] 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 PubMedCellular systems for handling transition metal ions have been identified, but little is known about the structure and function of the specific trafficking proteins. The 1.8 A resolution structure of the yeast copper chaperone for superoxide dismutase (yCCS) reveals a protein composed of two domains. The N-terminal domain is very similar to the metallochaperone protein Atx1 and is likely to play a role in copper delivery and/or uptake. The second domain resembles the physiological target of yCCS, superoxide dismutase I (SOD1), in overall fold, but lacks all of the structural elements involved in catalysis. In the crystal, two SOD1-like domains interact to form a dimer. The subunit interface is remarkably similar to that in SOD1, suggesting a structural basis for target recognition by this metallochaperone. Crystal structure of the copper chaperone for superoxide dismutase.,Lamb AL, Wernimont AK, Pufahl RA, Culotta VC, O'Halloran TV, Rosenzweig AC Nat Struct Biol. 1999 Aug;6(8):724-9. PMID:10426947[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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