1cc7

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[[Image:1cc7.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN==
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|PDB= 1cc7 |SIZE=350|CAPTION= <scene name='initialview01'>1cc7</scene>, resolution 1.20&Aring;
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<StructureSection load='1cc7' size='340' side='right'caption='[[1cc7]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>
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<table><tr><td colspan='2'>[[1cc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CC7 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene></td></tr>
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|DOMAIN=
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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=1cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cc7 OCA], [https://pdbe.org/1cc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cc7 RCSB], [https://www.ebi.ac.uk/pdbsum/1cc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cc7 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cc7 OCA], [http://www.ebi.ac.uk/pdbsum/1cc7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cc7 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cc/1cc7_consurf.spt"</scriptWhenChecked>
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BACKGROUND: Metallochaperone proteins function in the trafficking and delivery of essential, yet potentially toxic, metal ions to distinct locations and particular proteins in eukaryotic cells. The Atx1 protein shuttles copper to the transport ATPase Ccc2 in yeast cells. Molecular mechanisms for copper delivery by Atx1 and similar human chaperones have been proposed, but detailed structural characterization is necessary to elucidate how Atx1 binds metal ions and how it might interact with Ccc2 to facilitate metal ion transfer. RESULTS: The 1.02 A resolution X-ray structure of the Hg(II) form of Atx1 (HgAtx1) reveals the overall secondary structure, the location of the metal-binding site, the detailed coordination geometry for Hg(II), and specific amino acid residues that may be important in interactions with Ccc2. Metal ion transfer experiments establish that HgAtx1 is a functional model for the Cu(I) form of Atx1 (CuAtx1). The metal-binding loop is flexible, changing conformation to form a disulfide bond in the oxidized apo form, the structure of which has been solved to 1.20 A resolution. CONCLUSIONS: The Atx1 structure represents the first structure of a metallochaperone protein, and is one of the largest unknown structures solved by direct methods. The structural features of the metal-binding site support the proposed Atx1 mechanism in which facile metal ion transfer occurs between metal-binding sites of the diffusible copper-donor and membrane-tethered copper-acceptor proteins. The Atx1 structural motif represents a prototypical metal ion trafficking unit that is likely to be employed in a variety of organisms for different metal ions.
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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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==About this Structure==
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</jmolCheckbox>
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1CC7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CC7 OCA].
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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=1cc7 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution., Rosenzweig AC, Huffman DL, Hou MY, Wernimont AK, Pufahl RA, O'Halloran TV, Structure. 1999 Jun 15;7(6):605-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10404590 10404590]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Hou TVO]]
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[[Category: Hou, T V.O.]]
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[[Category: Huffman DL]]
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[[Category: Huffman, D L.]]
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[[Category: Pufahl MYRA]]
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[[Category: Pufahl, M Y.R A.]]
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[[Category: Rosenzweig AC]]
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[[Category: Rosenzweig, A C.]]
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[[Category: Wernimont AK]]
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[[Category: Wernimont, A K.]]
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[[Category: copper transport]]
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[[Category: mercury coordination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:47 2008''
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Current revision

CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN

PDB ID 1cc7

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