1fe0

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[[Image:1fe0.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF CADMIUM-HAH1==
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|PDB= 1fe0 |SIZE=350|CAPTION= <scene name='initialview01'>1fe0</scene>, resolution 1.75&Aring;
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<StructureSection load='1fe0' size='340' side='right'caption='[[1fe0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
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<table><tr><td colspan='2'>[[1fe0]] is a 2 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=1FE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FE0 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]] 1.75&#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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1fe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fe0 OCA], [https://pdbe.org/1fe0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fe0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fe0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fe0 ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF CADMIUM-HAH1'''
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== Function ==
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[https://www.uniprot.org/uniprot/ATOX1_HUMAN ATOX1_HUMAN] Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The Hah1 metallochaperone protein is implicated in copper delivery to the Menkes and Wilson disease proteins. Hah1 and the N-termini of its target proteins belong to a family of metal binding domains characterized by a conserved MT/HCXXC sequence motif. The crystal structure of Hah1 has been determined in the presence of Cu(I), Hg(II), and Cd(II). The 1.8 A resolution structure of CuHah1 reveals a copper ion coordinated by Cys residues from two adjacent Hah1 molecules. The CuHah1 crystal structure is the first of a copper chaperone bound to copper and provides structural support for direct metal ion exchange between conserved MT/HCXXC motifs in two domains. The structures of HgHah1 and CdHah1, determined to 1.75 A resolution, also reveal metal ion coordination by two MT/HCXXC motifs. An extended hydrogen bonding network, unique to the complex of two Hah1 molecules, stabilizes the metal binding sites and suggests specific roles for several conserved residues. Taken together, the structures provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1fe0_consurf.spt"</scriptWhenChecked>
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1FE0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FE0 OCA].
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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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==Reference==
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</jmolCheckbox>
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Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins., Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC, Nat Struct Biol. 2000 Sep;7(9):766-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10966647 10966647]
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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=1fe0 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: Huffman DL]]
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[[Category: Huffman, D L.]]
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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: 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: CD]]
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[[Category: SO4]]
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[[Category: SUC]]
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[[Category: beta-alpha-beta-beta-alpha-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:07:55 2008''
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Current revision

CRYSTAL STRUCTURE OF CADMIUM-HAH1

PDB ID 1fe0

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