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2za6

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Revision as of 09:34, 17 October 2018

recombinant horse L-chain apoferritin

Structural highlights

2za6 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2za7, 2za8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yoshizawa K, Mishima Y, Park SY, Heddle JG, Tame JR, Iwahori K, Kobayashi M, Yamashita I. Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment. J Biochem. 2007 Dec;142(6):707-13. Epub 2007 Oct 15. PMID:17938140 doi:10.1093/jb/mvm187

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2za6"

@@ Line 1: / Line 1: @@
 ==recombinant horse L-chain apoferritin==
 <StructureSection load='2za6' size='340' side='right' caption='[[2za6]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za7|2za7]], [[2za8|2za8]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za6 OCA], [http://pdbe.org/2za6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za6 RCSB], [http://www.ebi.ac.uk/pdbsum/2za6 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2za6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za6 OCA], [http://pdbe.org/2za6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za6 RCSB], [http://www.ebi.ac.uk/pdbsum/2za6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2za6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2za6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2za6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 41: / Line 42: @@
 [[Category: Tame, J R.H]]
 [[Category: Yamashita, I]]
+[[Category: Acetylation]]
 [[Category: Ferric iron binding]]
 [[Category: Iron storage]]
 [[Category: Metal binding protein]]
 [[Category: Metal-binding]]

2za6

From Proteopedia

Revision as of 09:34, 17 October 2018

recombinant horse L-chain apoferritin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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