Bacterioferritins and ferritins are distantly related in evolution. Conservation of ferroxidase-centre residues
- PMID: 1959654
- DOI: 10.1016/0014-5793(91)81177-a
Bacterioferritins and ferritins are distantly related in evolution. Conservation of ferroxidase-centre residues
Abstract
Iron-storage proteins can be divided into two classes; the bacterioferritins and ferritins. In spite of many apparent structural and functional analogies, no significant amino acid sequence similarity has been detected previously. This report now reveals a distant evolutionary relationship between bacterioferritins and ferritins derived by 'Profile Analysis'. Optimum alignment of bacterioferritin and ferritin sequences suggests that key residues of the ferroxidase centres of ferritins are conserved in bacterioferritins.
Similar articles
-
Unification of the ferritin family of proteins.Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2419-23. doi: 10.1073/pnas.89.6.2419. Proc Natl Acad Sci U S A. 1992. PMID: 1549605 Free PMC article.
-
Electron Transfer from Haem to the Di-Iron Ferroxidase Centre in Bacterioferritin.Angew Chem Int Ed Engl. 2021 Apr 6;60(15):8376-8379. doi: 10.1002/anie.202015965. Epub 2021 Mar 1. Angew Chem Int Ed Engl. 2021. PMID: 33460502 Free PMC article.
-
Serendipitous crystallization and structure determination of bacterioferritin from Achromobacter.Acta Crystallogr F Struct Biol Commun. 2018 Sep 1;74(Pt 9):558-566. doi: 10.1107/S2053230X18009809. Epub 2018 Aug 29. Acta Crystallogr F Struct Biol Commun. 2018. PMID: 30198888 Free PMC article.
-
Iron storage in bacteria.Adv Microb Physiol. 1998;40:281-351. doi: 10.1016/s0065-2911(08)60134-4. Adv Microb Physiol. 1998. PMID: 9889981 Review.
-
Structure, function, and evolution of ferritins.J Inorg Biochem. 1992 Aug 15-Sep;47(3-4):161-74. doi: 10.1016/0162-0134(92)84062-r. J Inorg Biochem. 1992. PMID: 1431878 Review.
Cited by
-
Ferritin gene organization: differences between plants and animals suggest possible kingdom-specific selective constraints.J Mol Evol. 1996 Mar;42(3):325-36. doi: 10.1007/BF02337543. J Mol Evol. 1996. PMID: 8661994
-
Characterization of a Helicobacter pylori neutrophil-activating protein.Infect Immun. 1995 Jun;63(6):2213-20. doi: 10.1128/iai.63.6.2213-2220.1995. Infect Immun. 1995. PMID: 7768601 Free PMC article.
-
Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.Biochem J. 2000 Aug 1;349 Pt 3(Pt 3):783-6. doi: 10.1042/bj3490783. Biochem J. 2000. PMID: 10903139 Free PMC article.
-
Bacterioferritin A modulates catalase A (KatA) activity and resistance to hydrogen peroxide in Pseudomonas aeruginosa.J Bacteriol. 1999 Jun;181(12):3730-42. doi: 10.1128/JB.181.12.3730-3742.1999. J Bacteriol. 1999. PMID: 10368148 Free PMC article.
-
Paracrystalline inclusions of a novel ferritin containing nonheme iron, produced by the human gastric pathogen Helicobacter pylori: evidence for a third class of ferritins.J Bacteriol. 1993 Feb;175(4):966-72. doi: 10.1128/jb.175.4.966-972.1993. J Bacteriol. 1993. PMID: 8432720 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases