Ferritin

From Proteopedia

Revision as of 10:02, 15 May 2017

spinqualitylabelsall models Crystal structure of Fe-soaked ferritin from the hyperthermophilic archael anaerobe Pyrococcus furiousus, 2jd7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Function

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).^[1] Amphibians have an additional middle subunit FR (FTM).

• 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) - a ferritin-like diiron carboxylate.
  
• MrgA – another iron storage protein - belongs to the Dps family.

Relevance

Cavities formed by FR are used for the manufacture of nanoparticles. FR is used as a marker for iron overload disorder.

Disease

FR deficiency can lead to anemia.

3D Structures of Ferritin

Updated on 15-May-2017 {{#tree:id=OrganizedByTopic|openlevels=0|

• Ferritin

• • 2jd6, 2jd7 – PfFR - Pyrococcus furiosus
    
  • 2jd8 – PfFR+Zn
    
  • 3a68 – soFR from gene SferH4 – soybean
    
  • 3a9q - soFR from gene SferH4 (mutant)
    
  • 3egm, 3bvf, 3bvi, 3bvk, 3bvl – HpFR – Heliobacter pylori
    
  • 5c6f – HpFR (mutant) + Fe
    
  • 1z4a, 1vlg – FR – Thermotoga maritime
    
  • 1s3q, 1sq3, 3kx9 – FR – Archaeoglubus fulgidus
    
  • 1krq – FR – Campylobacter jejuni
    
  • 1eum - EcFR – Escherichia coli
    
  • 4reu – EcFR + Fe
    
  • 4xgs – EcFR (mutant) + Fe2O2
    
  • 4ztt – EcFR (mutant) + Fe2O + Fe2 + Fe + O2
    
  • 1qgh – LiFR - Listeria innocua
    
  • 3qz3 - VcFR – Vibrio cholerae
    
  • 3vnx – FR – Ulva pertusa
    
  • 4ism, 4isp, 4itt, 4itw, 4iwj, 4iwk, 4ixk, 3e6s – PnmFR – Pseudo-nitschia multiseries
    
  • 4zkh, 4zkw, 4zkx, 4zl5, 4zl6, 4zlw, 4zmc – PnmFR (mutant) + Fe
    
  • 1z6o – FR – Trichoplusia ni
    
  • 4cmy – FR + Fe – Chlorobaculum tepidum
    

• Ferritin light chain (FTL)

• • 1lb3, 1h96 – mFTL – mouse
    
  • 1rcc, 1rcd, 1rci – bFTL+tartrate+Mg
    
  • 1rce, 1rcg - bFTL+tartrate+Mn
    
  • 3noz, 3np0, 3np2, 3o7r – hoFTL (mutant) - horse
    
  • 3o7s, 3u90 - hoFTL
    
  • 4v1w – hoFTL – cryo EM
    
  • 3rav, 3rd0 – hoFTL + barbiturate

• Ferritin middle subunit (FTM)

• • 4das – bFTM - bullfrog
    
  • 4p18 – bFTM (mutant)
    
  • 4lpj, 4lqj, 4lqn, 4lqv, 4lyu, 4lyx, 4my7, 3rbc, 3rgd – bFTM + Fe
    
  • 4mjy, 4ml5, 4mn9, 5j8w, 5j93, 5j9v, 5jac – bFTM (mutant) + Fe
    
  • 4lqh, 1mfr, [[3ka3] – bFTM + Mg
    
  • 4lpm, 4mku, 5j8s, 3se1, 3sh6, 3shx – bFTM (mutant) + Mg
    
  • 3ka4 – bFTM + Co
    
  • 4lpn, 3ka8, 3ka6, 3ka9 – bFTM (mutant) + Co
    
  • 1bg7 – bFTM + Ca
    
  • 3re7 – bFTM + Cu
    

• apo-ferritin (apo-FR)

• • 2x17 – apo-PfFR+Ag
    
  • 3h7g – apo-hoFR+Au
    
  • 1hrs - apo-hoFR+protoporphyrin
    
  • 3bve – apo-HpFR
    
  • 3e6r – apo-PnFR
    
  • 2clu, 2cn6 - apo-hFR (mutant)+Zn - human
    

• apo-ferritin light chain (apo-FTL)

• • 2zg7, 2z5p, 2z5q, 2z5r, 3fi6, 3af7, 5e2d, 5hqo – apo-hoFTL+Pd
    
  • 2zg8, 2zg9, 3af8, 3af9, 3noz, 3np0, 3np2 - apo-hoFTL (mutant)+Pd
    
  • 3o7s, 3wvw - apo-hoFTL+Ru
    
  • 3o7r, 3wvu, 3wvv - apo-hoFTL (mutant) + Ru
    
  • 4z3b - apo-hoFTL + Mn
    
  • 5axs, 5e1u, 5erj, 5erk, 5ix6, 5mij, 5mik - apo-hoFTL + Cd
    
  • 5lg2 - apo-hoFTL + Fe
    
  • 5czu - apo-hoFTL (mutant) + Fe
    
  • 3f33, 3f34, 3f35, 3f36, 3f37, 3f38, 3f39 - apo-hoFTL+phenols
    
  • 2v2i, 2v2j - apo-hoFTL+haemin
    
  • 2gyd - apo-hoFTL+diaziflurane
    
  • 1xz1 - apo-hoFTL+halothane
    
  • 1xz3 - apo-hoFTL+isoflurane
    
  • 1gwg - apo-hoFTL+I3
    
  • 2v2l, 2v2m, 2v2n, 2v2o, 2v2p, 2v2r, 2v2s - apo-hoFTL (mutant)+haemin
    
  • 2za6, 2g4h, 1aew, 1dat, 1ier, 1ies, 3f32, 2zur, 2w0o - apo-hoFTL
    
  • 2fg8 – apo-hFTL + Cs
    
  • 3kxu, 2ffx, 2fg4 - apo-hFTL+ Cd
    
  • 1fha, 5lg8 - apo-hFTL+ Fe
    
  • 4de6 - apo-hoFTL + arachidonic acid

• apo-ferritin heavy chain (apo-FTH)

• • 2za7, 2za8, 2cn7, 2chi, 2clu - apo-hoFTH (mutant)
    
  • 2cei, 2cih, 2cn6, 2iu2 - apo-hoFTH (mutant)+Zn
    
  • 5gu0, 5gu1, 5gu2, 5gu3 - apo-hoFTH (mutant) + Cd
    
  • 3erz – apo-hFR+Hg
    
  • 3es3 - apo-hFR+Au
    
  • 5gou – hFTH
    
  • 4oyn, 4y08, 4zjk, 5jkk, 5jkl, 5jkm – hFTH + Fe
    
  • 2z6m – hFTH + Zn
    
  • 5cmq, 5cmr - hFTH (mutant) + Zn
    
  • 1r03, 3ajo – hFTH + Mg
    
  • 2fha – hFTH + Ca
    
  • 4dyx, 4dyy, 4dyz, 4dz0 - hFTH (mutant) + Cu
    
  • 3ajp, 3ajq - hFTH (mutant) + Mg
    
  • 3wnw – mFTH + Fe
    

• Ferritin light+heavy chains

• • 5gn8 – hFTH + Ca
    

• Bacterioferritin (BFR)

• • 3gvy – BFR – Rhodobacter sphaeroides
    
  • 1jgc - BFR – Rhodobacter capsulatus
    
  • 1ji4 – BFR – Helicobacter pylori
    
  • 1nf4, 1nf6, 1nfv – BFR – Desulfovibrio desulfuricans
    
  • 3fvb – BmBFR - Brucelia melitensis
    
  • 2fkz, 2fl0, 1sof – BFR – Azotobacrter vinelandii
    
  • 2wtl, 3qb9, 3uof, 3uoi – BFR – Mycobacterium tuberculosis
    
  • 3bkn - MsBFR – Mycobacterium smegmatis
    
  • 3is7, 3is8, 3ise, 3isf, 3r2h, 3r2k, 3r2l, 3r2m, 3r2o, 3r2r, 3r2s – BFR – Pseudomonas aeruginosa
    
  • 1bfr, 1bcf, 2htn, 2vxi, 3e1j, 3e1l, 3e1m, 3e1n, 3e1p, 3e1o, 3e1q, 2y3q – EcBFR
    
  • 3e2c, 4cvr, 4cvt – EcBFR (mutant) + Zn
    
  • 4cvp, 3ghq - EcBFR (mutant) + Fe
    
  • 4cvs – EcBFR (mutant) + Cd
    
  • 4am2, 4am4, 4am5 – BFR + Fe – Blastochloris viridis

• Thioferritin (TFR)

• • 2vzb – TFR – Bacterioides fragilis

• DNA-binding Protein of Starved cells (Dps)

• • 3iq1 – VcDps
    
  • 3ge4 – BmDps
    
  • 2iy4 – Dps + Fe – Listeria monocytogenes
    
  • 2bkc, 2bk6, 2bjy – LiDps (mutant)
    
  • 2f7n – Dps + Co – Deinococcus radiodurans
    
  • 4a25 - Dps + Mn – Kinecoccus radiodurans
    
  • 1tjo, 1tk6, 1tkp, 1tko, 1moj – Dps + Fe – Halobacterium salinarum
    
  • 1o9r – Dps + Fe – Agrobacterium tumefaciens
    
  • 1dps, 1f33 – EcDps
    
  • 1f30 – EcDps + Zn
    
  • 1jre – EcDps + Cd
    
  • 1jts, 1l8h, 1l8i – EcDps (mutant)
    
  • 2ux1 – SsDps + Zn – Streptococcus suis
    
  • 2v15 – SsDps + Te
    
  • 2xjm – SsDps + Co
    
  • 2xjn – SsDps + Cu
    
  • 2xjo – SsDps + Ni
    
  • 2xkq – SsDps + Mn
    
  • 2yw6, 2yw7 – MsDps
    
  • 3ak8, 3ak9 – Dps + Mg – Salmonella enterica
    
  • 1n1q – Dps + Fe2O– Brevibacillus brevis
    
  • 1vei, 1vel, 1veq – MsDps + Fe
    
  • 4dyu – Dps + Zn – Yersinia pestis
    
  • 5hjf - NpDps – Nostoc punctiforme
    
  • 5i4j - NpDps + Zn
    
  • 5h4h - NpDps + Fe
    

• MrgA

• • 2chp – MrgA – Bacillus subtilis
    

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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