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1bg7

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LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?

Structural highlights

1bg7 is a 1 chain structure with sequence from Lithobates catesbeianus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FRI1_LITCT Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.^[1]

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

How and where iron exits from ferritin for cellular use is unknown. Twenty-four protein subunits create a cavity in ferritin where iron is concentrated >10(11)-fold as a mineral. Proline substitution for conserved leucine 134 (L134P) allowed normal assembly but increased iron exit rates. X-ray crystallography of H-L134P ferritin revealed localized unfolding at the 3-fold axis, also iron entry sites, consistent with shared use sites for iron exit and entry. The junction of three ferritin subunits appears to be a dynamic aperture with a "shutter" that cytoplasmic factors might open or close to regulate iron release in vivo.

Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?,Takagi H, Shi D, Ha Y, Allewell NM, Theil EC J Biol Chem. 1998 Jul 24;273(30):18685-8. PMID:9668036^[2]

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

References

↑ Takagi H, Shi D, Ha Y, Allewell NM, Theil EC. Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J Biol Chem. 1998 Jul 24;273(30):18685-8. PMID:9668036
↑ Takagi H, Shi D, Ha Y, Allewell NM, Theil EC. Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J Biol Chem. 1998 Jul 24;273(30):18685-8. PMID:9668036

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/1bg7"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bg7' size='340' side='right'caption='[[1bg7]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bg7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/American_bullfrog American bullfrog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BG7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lithobates_catesbeianus Lithobates catesbeianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BG7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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=1bg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg7 OCA], [http://pdbe.org/1bg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bg7 RCSB], [http://www.ebi.ac.uk/pdbsum/1bg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg7 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg7 OCA], [https://pdbe.org/1bg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bg7 RCSB], [https://www.ebi.ac.uk/pdbsum/1bg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FRI1_LITCT FRI1_LITCT]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.<ref>PMID:9668036</ref>
+[https://www.uniprot.org/uniprot/FRI1_LITCT FRI1_LITCT] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.<ref>PMID:9668036</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: American bullfrog]]
 [[Category: Large Structures]]
-[[Category: Allewell, N M]]
+[[Category: Lithobates catesbeianus]]
-[[Category: Ha, Y]]
+[[Category: Allewell NM]]
-[[Category: Shi, D]]
+[[Category: Ha Y]]
-[[Category: Takagi, H]]
+[[Category: Shi D]]
-[[Category: Theil, E C]]
+[[Category: Takagi H]]
-[[Category: Ferritin]]
+[[Category: Theil EC]]
-[[Category: Iron storage]]

1bg7

From Proteopedia

Current revision

LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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