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2za7

From Proteopedia

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Revision as of 12:00, 29 July 2020

recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-4)

Structural highlights

2za7 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.
Related:	2za6, 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/2za7"

@@ Line 1: / Line 1: @@
 ==recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-4)==
-<StructureSection load='2za7' size='340' side='right' caption='[[2za7]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<StructureSection load='2za7' size='340' side='right'caption='[[2za7]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2za7]] is a 1 chain structure 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=2ZA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZA7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2za7]] is a 1 chain structure 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=2ZA7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZA7 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za6|2za6]], [[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=2za7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za7 OCA], [http://pdbe.org/2za7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za7 RCSB], [http://www.ebi.ac.uk/pdbsum/2za7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2za7 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2za7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za7 OCA], [http://pdbe.org/2za7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2za7 RCSB], [http://www.ebi.ac.uk/pdbsum/2za7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2za7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Ferritin|Ferritin]]
+*[[Ferritin 3D structures|Ferritin 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Equus caballus]]
+[[Category: Large Structures]]
 [[Category: Heddle, J G]]
 [[Category: Mishima, Y]]

2za7

From Proteopedia

Revision as of 12:00, 29 July 2020

recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-4)

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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