1aew

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[[Image:1aew.gif|left|200px]]
 
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==L-CHAIN HORSE APOFERRITIN==
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The line below this paragraph, containing "STRUCTURE_1aew", creates the "Structure Box" on the page.
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<StructureSection load='1aew' size='340' side='right'caption='[[1aew]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1aew]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. The November 2002 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Ferritin and Transferrin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2002_11 10.2210/rcsb_pdb/mom_2002_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AEW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.95&#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></td></tr>
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{{STRUCTURE_1aew| PDB=1aew | SCENE= }}
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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=1aew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aew OCA], [https://pdbe.org/1aew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aew RCSB], [https://www.ebi.ac.uk/pdbsum/1aew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aew 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/ae/1aew_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=1aew ConSurf].
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<div style="clear:both"></div>
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'''L-CHAIN HORSE APOFERRITIN'''
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==See Also==
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*[[Ferritin 3D structures|Ferritin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Mammalian ferritins are 24-mers assembled from two types of polypeptide chain which provide the molecule with different functions. H(eavy) chains catalyse the first step in iron storage, the oxidation of iron(II). L(ight) chains promote the nucleation of the mineral ferrihydrite enabling storage of iron(III) inside the protein shell. We report here the comparison of the three-dimensional structures of recombinant human H chain (HuHF) and horse L chain (HoLF) ferritin homopolymers, which have been refined at 1.9 A resolution. There is 53% sequence identity between these molecules, and the two structures are very similar, the H and L subunit alpha-carbons superposing to within 0.5 A rms deviation with 41 water molecules in common. Nevertheless, there are significant important differences which can be related to differences in function. In particular, the centres of the four-helix bundles contain distinctive groups of hydrophilic residues which have been associated with ferroxidase activity in H chains and enhanced stability in L chains. L chains contain a group of glutamates associated with mineralisation within the iron storage cavity of the protein.
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==About this Structure==
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1AEW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. The following page contains interesting information on the relation of 1AEW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb35_1.html Ferritin and Transferrin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEW OCA].
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==Reference==
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Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9159481 9159481]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Ferritin and Transferrin]]
[[Category: Ferritin and Transferrin]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Artymiuk, P J.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Harrison, P M.]]
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[[Category: Artymiuk PJ]]
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[[Category: Hempstead, P D.]]
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[[Category: Harrison PM]]
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[[Category: Lawson, D M.]]
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[[Category: Hempstead PD]]
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[[Category: Yewdall, S J.]]
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[[Category: Lawson DM]]
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[[Category: Acetylation]]
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[[Category: Yewdall SJ]]
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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 Fri May 2 10:10:39 2008''
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Current revision

L-CHAIN HORSE APOFERRITIN

PDB ID 1aew

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