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1do5

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(New page: 200px<br /> <applet load="1do5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1do5, resolution 2.75&Aring;" /> '''HUMAN COPPER CHAPER...)
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[[Image:1do5.gif|left|200px]]<br />
 
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<applet load="1do5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1do5, resolution 2.75&Aring;" />
 
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'''HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE DOMAIN II'''<br />
 
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==Overview==
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==HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE DOMAIN II==
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The human copper chaperone for superoxide dismutase (hCCS) delivers the, essential copper ion cofactor to copper,zinc superoxide dismutase (SOD1), a key enzyme in antioxidant defense. Mutations in SOD1 are linked to, familial amyotrophic lateral sclerosis (FALS), a fatal neurodegenerative, disorder. The molecular mechanisms by which SOD1 is recognized and, activated by hCCS are not understood. To better understand this, biochemical pathway, we have determined the X-ray structure of the largest, domain of hCCS (hCCS Domain II) to 2. 75 A resolution. The overall, structure is closely related to that of its target enzyme SOD1, consisting, of an eight-stranded beta-barrel and a zinc-binding site formed by two, extended loops. The first of these loops provides the ligands to a bound, zinc ion, and is analogous to the zinc subloop in SOD1. The second, structurally resembles the SOD1 electrostatic channel loop, but lacks many, of the residues important for catalysis. Like SOD1 and yCCS, hCCS forms a, dimer using a highly conserved interface. In contrast to SOD1, however, the hCCS structure does not contain a copper ion bound in the catalytic, site. Notably, the structure reveals a single loop proximal to the dimer, interface which is unique to the CCS chaperones.
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<StructureSection load='1do5' size='340' side='right'caption='[[1do5]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1do5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DO5 FirstGlance]. <br>
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Known disease associated with this structure: Asthma, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=192020 192020]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==About this Structure==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1do5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1do5 OCA], [https://pdbe.org/1do5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1do5 RCSB], [https://www.ebi.ac.uk/pdbsum/1do5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1do5 ProSAT]</span></td></tr>
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1DO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DO5 OCA].
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</table>
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== Function ==
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==Reference==
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[https://www.uniprot.org/uniprot/CCS_HUMAN CCS_HUMAN] Delivers copper to copper zinc superoxide dismutase (SOD1).
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Crystal structure of the second domain of the human copper chaperone for superoxide dismutase., Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC, Biochemistry. 2000 Feb 22;39(7):1589-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10677207 10677207]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1do5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1do5 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Halloran, T.V.O.]]
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[[Category: Lamb AL]]
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[[Category: Lamb, A.L.]]
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[[Category: O'Halloran TV]]
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[[Category: Pufahl, R.A.]]
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[[Category: Pufahl RA]]
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[[Category: Rosenzweig, A.C.]]
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[[Category: Rosenzweig AC]]
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[[Category: Wernimont, A.K.]]
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[[Category: Wernimont AK]]
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[[Category: ZN]]
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[[Category: beta-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:34:14 2007''
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Current revision

HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE DOMAIN II

PDB ID 1do5

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