Ferritin

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[[Image:2jd73.png|thumb|left|250px|Crystal structure of ferritin from ''Pyrococcs Furiousus'' ([[2jd7]])]]
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<StructureSection load='' size='400' side='right' caption="Crystal structure of Fe-soaked ferritin from the hyperthermophilic archael anaerobe ''Pyrococcus furiousus'' [[2jd7]]" scene='Ferritin/Starting_ferritin_scene/1'>
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<applet load='Pdb2jd7.pdb' size='350' frame='true' align='right' scene="Ferritin/Starting_ferritin_scene/1" caption="Crystal structure of Fe-soaked ferritin from the hyperthermophilic archael anaerobe ''Pyrococcus furiousus'', [[2jd7]]" />
 
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[[Ferritin]] (FR) is an iron storage and release protein. It stores iron as microcrystals with phosphate and hydroxide ions. FR is composed of 24 subunits of heavy chain (FTH) and light chain (FTL). Bacterioferritin (BFR) structure is very similar to FR. It contains a binuclear iron center and haem. It stores iron as ferric oxide mineral in its hollow central cavity. Thioferritin (TFR) is a ferritin-related protein with 2 Cysteine residues adjacent to the dimetal binding site. Another iron storing protein is the DNA-binding Protein of Starved cells (Dps). MrgA – another iron storage protein - belongs
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== Function ==
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to the Dps family.
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{{Clear}}
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[[Ferritin]] (FR) is an iron storage and release protein. It stores iron as microcrystals with phosphate and hydroxide ions. FR is composed of 24 subunits of heavy chain (FTH) and light chain (FTL).<ref>PMID:20304033</ref> Amphibians have an additional middle subunit FR (FTM).<br />
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==3D Structures of Ferritin==
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* '''apo-ferritin''' (apo-FR) is a non-Fe-containing ferritin.<br />
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* '''Bacterioferritin''' (BFR) structure is very similar to FR. It contains a binuclear iron center and haem. It stores iron as ferric oxide mineral in its hollow central cavity<ref>PMID:37375226</ref>.<br />
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* '''Thioferritin''' (TFR) is a ferritin-related protein with 2 cysteine residues adjacent to the dimetal binding site.<br />
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* '''DNA-binding Protein of Starved cells''' (Dps) - a ferritin-like diiron carboxylate which acts as a molecular chaperone and may confer thermotolerance in ''E. coli''<ref>PMID:37229826</ref>.<br />
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===Ferritin===
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== Relevance ==
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[[2jd6]], [[2jd7]] – PfFR - Pyrococcus furiosus <br />
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Cavities formed by FR are used for the manufacture of nanoparticles. FR is used as a marker for iron overload disorder.
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[[2jd8]] – PfFR+Zn<br />
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[[3kxu]] – hFR (mutant) – human<br />
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[[3hx2]], [[3hx5]], [[3hx7]] - hFR<br />
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[[3a68]] – soFR from gene SferH4 – soybean<br />
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[[3a9q]] - soFR from gene SferH4 (mutant) <br />
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[[3egm]], [[3bvf]], [[3bvi]], [[3bvk]], [[3bvl]] – HpFR – Heliobacter pylori<br />
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[[3e6s]] - PnFR – Pseudo-nitzschia<br />
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[[1z4a]], [[1vlg]] – FR – Thermotoga maritime<br />
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[[1s3q]], [[1sq3]] – FR – Archaeoglubus fulgidus<br />
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[[1krq]] – FR – Campylobacter jejuni<br />
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[[1eum]] - EcFR – Escherichia coli<br />
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[[1qgh]] – LiFR - Listeria innocua<br />
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[[1mfr]], [[1bg7]] – bFR - Bullfrog<br />
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===Ferritin light chain (FTL) ===
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== Disease ==
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[[1lb3]], [[1h96]] – FTL – mouse<br />
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FR deficiency can lead to anemia.
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[[1rcc]], [[1rcd]], [[1rci]] – bFTL+tartrate+Mg<br />
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[[1rce]], [[1rcg]] - bFTL+tartrate+Mn<br />
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===Ferritin heavy chain (FTH) ===
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==3D Structures of Ferritin==
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[[Ferritin 3D structures]]
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[[2z6m]], [[1r03]], [[2fha]] – hFTH<br />
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[[2z6o]] – FTH – Trichoplusia ni<br />
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===apo-ferritin (apo-FR) ===
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[[2x17]] – apo-PfFR+Ag <br />
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[[3h7g]] – apo-hoFR+Au – horse<br />
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[[1hrs]] - apo-hoFR+protoporphyrin<br />
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[[3bve]] – apo-HpFR<br />
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[[3e6r]] – apo-PnFR <br />
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[[2clu]], [[2cn6]] - apo-hFR (mutant)+Zn<br />
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===apo-ferritin light chain (apo-FTL) ===
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[[2zg7]], [[2z5p]], [[2z5q]], [[2z5r]], [[3fi6]] – apo-hoFTL+Pd<br />
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[[2zg8]], [[2zg9]] - apo-hoFTL (mutant)+Pd<br />
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[[3f33]], [[3f34]], [[3f35]], [[3f36]], [[3f37]], [[3f38]], [[3f39]] - apo-hoFTL+phenols<br />
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[[2v2i]], [[2v2j]] - apo-hoFTL+haemin<br />
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[[2gyd]] - apo-hoFTL+diaziflurane<br />
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[[1xz1]] - apo-hoFTL+halothane<br />
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[[1xz3]] - apo-hoFTL+isoflurane<br />
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[[1gwg]] - apo-hoFTL+I3<br />
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[[2w0o]] – apo-hoFTL<br />
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[[2v2l]], [[2v2m]], [[2v2n]], [[2v2o]], [[2v2p]], [[2v2r]], [[2v2s]] - apo-hoFTL (mutant)+haemin<br />
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[[2za6]], [[2g4h]], [[1aew]], [[1dat]], [[1ier]], [[1ies]], [[3f32]], [[2zur]] - apo-hoFTL<br />
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[[2ffx]], [[2fg4]], [[2fg8]] – apo-hFTL<br />
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===apo-ferritin heavy chain (apo-FTH) ===
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[[2za7]], [[2za8]], [[2cn7]], [[2chi]], [[2clu]] - apo-hoFTH (mutant) <br />
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[[2cei]], [[2cih]], [[2cn6]], [[2iu2]] - apo-hoFTH (mutant)+Zn<br />
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[[3erz]] – apo-hFR+Hg<br />
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[[3es3]] - apo-hFR+Au<br />
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===Bacterioferritin (BFR) ===
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[[3gvy]] – BFR – Rhodobacter sphaeroides<br />
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[[3fvb]] – BmBFR - Brucelia melitensis<br />
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[[2fkz]], [[2fl0]] – BFR – Azotobacrter vinelandii<br />
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[[1bfr]] – EcBFR <br />
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===Thioferritin (TFR) ===
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[[2vzb]] – TFR – Bacterioides fragilis
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===DNA-binding Protein of Starved cells (Dps) ===
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</StructureSection>
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[[3iq1]] – Dps – Vibrio cholerae<br />
 
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[[3ge4]] – BmDps <br />
 
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[[2iy4]] – Dps – Listeria monocytogenes<br />
 
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[[2bkc]], [[2bk6]], [[2bjy]] – LiDps (mutant) <br />
 
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[[2f7n]] – Dps – Deinococcus radiodurans<br />
 
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[[1tjo]], [[1tk6]], [[1tkp]], [[1moj]] – Dps – Halobacterium salinarum<br />
 
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[[1o9r]] – Dps – Agrobacterium tumefaciens<br />
 
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[[1dps]] – EcDps <br />
 
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===MrgA===
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== References ==
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<references/>
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[[2chp]] – MrgA – Bacillus subtilis<br />
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[[Category:Topic Page]]

Current revision

Crystal structure of Fe-soaked ferritin from the hyperthermophilic archael anaerobe Pyrococcus furiousus 2jd7

Drag the structure with the mouse to rotate


References

  1. ↑ Wang W, Knovich MA, Coffman LG, Torti FM, Torti SV. Serum ferritin: Past, present and future. Biochim Biophys Acta. 2010 Aug;1800(8):760-9. doi: 10.1016/j.bbagen.2010.03.011. , Epub 2010 Mar 19. PMID:20304033 doi:http://dx.doi.org/10.1016/j.bbagen.2010.03.011
  2. ↑ van der Ven AM, Gyamfi H, Suttisansanee U, Ahmad MS, Su Z, Taylor RM, Poole A, Chiorean S, Daub E, Urquhart T, Honek JF. Molecular Engineering of E. coli Bacterioferritin: A Versatile Nanodimensional Protein Cage. Molecules. 2023 Jun 9;28(12):4663. PMID:37375226 doi:10.3390/molecules28124663
  3. ↑ Park JH, Lee ES, Jung YJ. Functional characterization of the DNA-binding protein from starved cells (DPS) as a molecular chaperone under heat stress. Biochem Biophys Res Commun. 2023 Jul 30;667:180-185. PMID:37229826 doi:10.1016/j.bbrc.2023.05.064

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