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1gwg

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[[Image:1gwg.gif|left|200px]]
 
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{{Structure
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==Tri-iodide derivative of apoferritin==
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|PDB= 1gwg |SIZE=350|CAPTION= <scene name='initialview01'>1gwg</scene>, resolution 2.01&Aring;
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<StructureSection load='1gwg' size='340' side='right'caption='[[1gwg]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
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|SITE= <scene name='pdbsite=CD1:Cd+Binding+Site+For+Chain+A'>CD1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>
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<table><tr><td colspan='2'>[[1gwg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWG 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]] 2.01&#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=IOD:IODIDE+ION'>IOD</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=1gwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwg OCA], [https://pdbe.org/1gwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwg RCSB], [https://www.ebi.ac.uk/pdbsum/1gwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwg 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=1gwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwg OCA], [http://www.ebi.ac.uk/pdbsum/1gwg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gwg RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
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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/gw/1gwg_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=1gwg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A series of experiments performed at Cu Kalpha wavelength on in-house X-ray equipment are presented which investigate two possibilities for enhancing the experimental phasing signal by means of (i) triiodide/iodide soaks using KI/I(2) and (ii) combinations of counter-ions introduced using the short cryosoak method. Triiodide-derivative crystal structures for five test proteins have been refined and reveal that iodine can bind as polyiodide and single iodide ions through hydrophobic and hydrogen-bonding interactions both at the molecular surface and in intramolecular and intermolecular cavities. In three cases, the structures could be automatically determined with autoSHARP using in-house SAD and SIRAS data. The investigation of combinatorial counter-ion replacement using multiple salts with Na(+) and Cs(+) as cations and I(-) and Cl(-) as anions reveals that, for the case of hen egg-white lysozyme, significant improvement in phasing signal is obtained by the combined use of salts compared with SIRAS methods using native and single short-soak derivative data sets.
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'''TRI-IODIDE DERIVATIVE OF APOFERRITIN'''
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Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment.,Evans G, Bricogne G Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:12037300<ref>PMID:12037300</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gwg" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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A series of experiments performed at Cu Kalpha wavelength on in-house X-ray equipment are presented which investigate two possibilities for enhancing the experimental phasing signal by means of (i) triiodide/iodide soaks using KI/I(2) and (ii) combinations of counter-ions introduced using the short cryosoak method. Triiodide-derivative crystal structures for five test proteins have been refined and reveal that iodine can bind as polyiodide and single iodide ions through hydrophobic and hydrogen-bonding interactions both at the molecular surface and in intramolecular and intermolecular cavities. In three cases, the structures could be automatically determined with autoSHARP using in-house SAD and SIRAS data. The investigation of combinatorial counter-ion replacement using multiple salts with Na(+) and Cs(+) as cations and I(-) and Cl(-) as anions reveals that, for the case of hen egg-white lysozyme, significant improvement in phasing signal is obtained by the combined use of salts compared with SIRAS methods using native and single short-soak derivative data sets.
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*[[Ferritin 3D structures|Ferritin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1GWG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWG OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment., Evans G, Bricogne G, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):976-91. Epub, 2002 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12037300 12037300]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bricogne, G.]]
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[[Category: Bricogne G]]
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[[Category: Evans, G.]]
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[[Category: Evans G]]
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[[Category: acetylation]]
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[[Category: iron storage]]
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[[Category: multigene family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:52:43 2008''
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Current revision

Tri-iodide derivative of apoferritin

PDB ID 1gwg

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