2za8

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[[Image:2za8.png|left|200px]]
 
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==recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-8)==
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The line below this paragraph, containing "STRUCTURE_2za8", creates the "Structure Box" on the page.
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<StructureSection load='2za8' size='340' side='right'caption='[[2za8]], [[Resolution|resolution]] 1.40&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'>[[2za8]] 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=2ZA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZA8 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]] 1.4&#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_2za8| PDB=2za8 | 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=2za8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za8 OCA], [https://pdbe.org/2za8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2za8 RCSB], [https://www.ebi.ac.uk/pdbsum/2za8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2za8 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/za/2za8_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=2za8 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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The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of 24 L-chain subunits, in acidic solution was studied. Using two rLF mutants, lacking four (Fer4) or eight (Fer8) N-terminal amino acid residues, the effect of N-terminal residues on the protein's stability was investigated. Of the two mutants and wild-type rLF, the tertiary and secondary structures of Fer8 were found to be most sensitive to an acidic environment. The Fer8 protein dissociated easily into subunit dimers at or below pH 2.0. Comparing the crystal structures of the mutant proteins, deletion of the N-terminal residues was found to result in fewer inter- and intra-subunit hydrogen bonds. The loss of these bonds is assumed to be responsible for lower endurance against acidic denaturation in N-terminus-deleted mutants. These results indicated that the inter- and intra-subunit hydrogen bonds of N-terminal residues affect the denaturation, especially oligomer formation of apoferritin subunits and will be of use in designing ferritin-based nanodevices.
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===recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-8)===
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Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment.,Yoshizawa K, Mishima Y, Park SY, Heddle JG, Tame JR, Iwahori K, Kobayashi M, Yamashita I J Biochem. 2007 Dec;142(6):707-13. Epub 2007 Oct 15. PMID:17938140<ref>PMID:17938140</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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The line below this paragraph, {{ABSTRACT_PUBMED_17938140}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2za8" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17938140 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17938140}}
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==About this Structure==
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[[2za8]] is a 1 chain structure of [[Ferritin]] with 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=2ZA8 OCA].
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==See Also==
==See Also==
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*[[Ferritin]]
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*[[Ferritin 3D structures|Ferritin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:17938140</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Heddle, J G.]]
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[[Category: Large Structures]]
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[[Category: Mishima, Y.]]
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[[Category: Heddle JG]]
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[[Category: Park, S Y.]]
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[[Category: Mishima Y]]
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[[Category: Tame, J R.H.]]
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[[Category: Park S-Y]]
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[[Category: Yamashita, I.]]
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[[Category: Tame JRH]]
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[[Category: Acetylation]]
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[[Category: Yamashita I]]
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[[Category: Ferric iron binding]]
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[[Category: Iron storage]]
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[[Category: Metal binding protein]]
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[[Category: Metal-binding]]
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Current revision

recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-8)

PDB ID 2za8

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