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1hrs

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[[Image:1hrs.gif|left|200px]]<br /><applet load="1hrs" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hrs, resolution 2.6&Aring;" />
 
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'''A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN'''<br />
 
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==Overview==
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==A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN==
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Ferritin, the iron-storage protein, binds porphyrins, metalloporphyrins and the fluorescent dyes ANS (8-anilino-1-naphthalenesulfonic acid) and TNS (2-p-toluidinyl-6-naphthalenesulfonic acid), similarly to apo-myoglobin. Octahedral crystals of horse-spleen apo-ferritin (HSF; 174 amino acids) complexes prepared by the addition of haem, hematoporphyrin or Sn-protoporphyrin IX to a solution of apo-ferritin crystallize in space group F432 with cell parameter a = 184.0 A. X-ray crystallographic analysis of single crystals prepared from a mixture containing haem or Sn-protoporphyrin IX shows that the haem-binding sites in these crystals are occupied by protoporphyrin IX, which is free of metal, rather than by the original metalloporphyrin. The present paper describes the structure of horse-spleen apo-ferritin cocrystallized with Sn-protoporphyrin IX. The 6797 reflections up to 2.6 A resolution used in the refinement were obtained from a data set recorded on a Nicolet/Xentronics area detector with Cu Kalpha radiation from a Rigaku RU 200 rotating anode. The final structure comprises 1613 non-H atoms, two Cd atoms and 170 solvent molecules. Four residues are described as disordered. The root-mean-square deviations from ideal bond lengths and angles are 0.013 A and 2.88 degrees, respectively. Protoporphyrins are observed in special positions on the twofold axes of the ferritin molecule with a stoichiometry of 0.4 per subunit.
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<StructureSection load='1hrs' size='340' side='right'caption='[[1hrs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hrs]] 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=1HRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRS FirstGlance]. <br>
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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]] 2.6&#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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PP9:PROTOPORPHYRIN+IX'>PP9</scene></td></tr>
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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=1hrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrs OCA], [https://pdbe.org/1hrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrs RCSB], [https://www.ebi.ac.uk/pdbsum/1hrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrs ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/hr/1hrs_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=1hrs ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HRS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=PP9:'>PP9</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRS OCA].
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*[[Ferritin 3D structures|Ferritin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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A crystallographic study of haem binding to ferritin., Precigoux G, Yariv J, Gallois B, Courseille C, d'Estaintot BL, Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):739-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299370 15299370]
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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: Courseille, C.]]
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[[Category: Courseille C]]
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[[Category: Dautant, A.]]
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[[Category: Dautant A]]
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[[Category: Estaintot, B Langlois D.]]
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[[Category: Gallois B]]
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[[Category: Gallois, B.]]
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[[Category: Langlois D'Estaintot B]]
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[[Category: Precigoux, G.]]
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[[Category: Precigoux G]]
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[[Category: Yariv, J.]]
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[[Category: Yariv J]]
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[[Category: CD]]
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[[Category: PP9]]
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[[Category: iron storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:14 2008''
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Current revision

A CRYSTALLOGRAPHIC STUDY OF HAEM BINDING TO FERRITIN

PDB ID 1hrs

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