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Volumn 106, Issue , 2014, Pages 39-47

The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family

Author keywords

Bacterial ferritin; Crystal structure; Ferroxidase center; HAADF STEM

Indexed keywords

BACTERIAL PROTEIN; CERULOPLASMIN; FERRITIN; RECOMBINANT PROTEIN; PROTEIN SUBUNIT;

EID: 84908021381     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.07.019     Document Type: Article
Times cited : (12)

References (49)
  • 2
    • 33751517409 scopus 로고    scopus 로고
    • High resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites
    • L. Toussaint, L. Bertrand, L. Hue, R.R. Crichton, and J.P. Declercq High resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites J. Mol. Biol. 365 2007 440 452
    • (2007) J. Mol. Biol. , vol.365 , pp. 440-452
    • Toussaint, L.1    Bertrand, L.2    Hue, L.3    Crichton, R.R.4    Declercq, J.P.5
  • 3
    • 0032793828 scopus 로고    scopus 로고
    • Crystal structure of bullfrog M ferritin at 2.8 A resolution: Analysis of subunit interactions and the binuclear metal center
    • Y. Ha, D. Shi, G.W. Small, E.C. Theil, and N.M. Allewell Crystal structure of bullfrog M ferritin at 2.8 A resolution: analysis of subunit interactions and the binuclear metal center J. Biol. Inorg. Chem. 4 1999 243 256
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 243-256
    • Ha, Y.1    Shi, D.2    Small, G.W.3    Theil, E.C.4    Allewell, N.M.5
  • 4
    • 0029040871 scopus 로고
    • High resolution crystal structures of amphibian red-cell L ferritin: Potential roles for structural plasticity and salvation in function
    • J. Trikha, E.C. Theil, and N.M. Allewell High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and salvation in function J. Mol. Biol. 248 1995 949 967
    • (1995) J. Mol. Biol. , vol.248 , pp. 949-967
    • Trikha, J.1    Theil, E.C.2    Allewell, N.M.3
  • 6
    • 77950463631 scopus 로고    scopus 로고
    • Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin
    • T. Masuda, F. Goto, T. Yoshihara, and B. Mikami Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin J. Biol. Chem. 285 2010 4049 4059
    • (2010) J. Biol. Chem. , vol.285 , pp. 4049-4059
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Mikami, B.4
  • 7
    • 19444383537 scopus 로고    scopus 로고
    • Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains
    • A.E. Hamburger, A.P. West Jr., Z.A. Hamburger, P. Hamburger, and P.J. Bjorkman Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains J. Mol. Biol. 349 2005 558 569
    • (2005) J. Mol. Biol. , vol.349 , pp. 558-569
    • Hamburger, A.E.1    West, A.P.2    Hamburger, Z.A.3    Hamburger, P.4    Bjorkman, P.J.5
  • 8
    • 0035937252 scopus 로고    scopus 로고
    • The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; Comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives
    • T.J. Stillman, P.D. Hempstead, P.J. Artymiuk, S.C. Andrews, A.J. Hudson, A. Treffry, J.R. Guest, and P.M. Harrison The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives J. Mol. Biol. 307 2001 587 603
    • (2001) J. Mol. Biol. , vol.307 , pp. 587-603
    • Stillman, T.J.1    Hempstead, P.D.2    Artymiuk, P.J.3    Andrews, S.C.4    Hudson, A.J.5    Treffry, A.6    Guest, J.R.7    Harrison, P.M.8
  • 9
    • 34249874901 scopus 로고    scopus 로고
    • Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus
    • J. Tatur, W.R. Hagen, and P.M. Matias Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus J. Biol. Inorg. Chem. 12 2007 615 630
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 615-630
    • Tatur, J.1    Hagen, W.R.2    Matias, P.M.3
  • 10
    • 17044381270 scopus 로고    scopus 로고
    • Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus
    • E. Johnson, D. Cascio, M.R. Sawaya, M. Gingery, and I. Schroder Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus Structure 13 2005 637 648
    • (2005) Structure , vol.13 , pp. 637-648
    • Johnson, E.1    Cascio, D.2    Sawaya, M.R.3    Gingery, M.4    Schroder, I.5
  • 11
    • 67349125435 scopus 로고    scopus 로고
    • The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake
    • K.J. Cho, H.J. Shin, J.H. Lee, K.J. Kim, S.S. Park, Y. Lee, C. Lee, S.S. Park, and K.H. Kim The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake J. Mol. Biol. 390 2009 83 98
    • (2009) J. Mol. Biol. , vol.390 , pp. 83-98
    • Cho, K.J.1    Shin, H.J.2    Lee, J.H.3    Kim, K.J.4    Park, S.S.5    Lee, Y.6    Lee, C.7    Park, S.S.8    Kim, K.H.9
  • 12
    • 79955523543 scopus 로고    scopus 로고
    • The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress
    • P. Ceci, E. Forte, G. Di Cecca, M. Fornara, and E. Chiancone The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress Extremophiles 15 2011 431 439
    • (2011) Extremophiles , vol.15 , pp. 431-439
    • Ceci, P.1    Forte, E.2    Di Cecca, G.3    Fornara, M.4    Chiancone, E.5
  • 13
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • A. Ilari, S. Stefanini, E. Chiancone, and D. Tsernoglou The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site Nat. Struct. Biol. 7 2000 38 43
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 15
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • B. Ren, G. Tibbelin, T. Kajino, O. Asami, and R. Ladenstein The multi-layered structure of Dps with a novel di-nuclear ferroxidase center J. Mol. Biol. 329 2003 467 477
    • (2003) J. Mol. Biol. , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 16
    • 79954538172 scopus 로고    scopus 로고
    • Ferritin structure from Mycobacterium tuberculosis: Comparative study with homologues identifies extended C-terminus involved in ferroxidase activity
    • G. Khare, V. Gupta, P. Nangpal, R.K. Gupta, N.K. Sauter, and A.K. Tyagi Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended C-terminus involved in ferroxidase activity PLoS One 6 2011 e18570 10.1371/journal.pone.0018570
    • (2011) PLoS One , vol.6 , pp. 18570
    • Khare, G.1    Gupta, V.2    Nangpal, P.3    Gupta, R.K.4    Sauter, N.K.5    Tyagi, A.K.6
  • 17
    • 84878234416 scopus 로고    scopus 로고
    • Mechanism of ferrous iron and oxidation by ferritin from a pennate diatom
    • S. Pfaffen, R. Abdulqadir, N.E. Le Brun, and M.E.P. Murphy Mechanism of ferrous iron and oxidation by ferritin from a pennate diatom J. Biol. Chem. 288 2013 14917 14925
    • (2013) J. Biol. Chem. , vol.288 , pp. 14917-14925
    • Pfaffen, S.1    Abdulqadir, R.2    Le Brun, N.E.3    Murphy, M.E.P.4
  • 18
    • 84922480881 scopus 로고    scopus 로고
    • Tale of tails: Deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor
    • [Epub ahead of print]
    • M.D. Hitchings, P. Townsend, E. Pohl, P.D. Facey, D.H. Jones, P.J. Dyson, and R. Del Sol Tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor Cell. Mol. Life Sci. 2014 [Epub ahead of print]
    • (2014) Cell. Mol. Life Sci.
    • Hitchings, M.D.1    Townsend, P.2    Pohl, E.3    Facey, P.D.4    Jones, D.H.5    Dyson, P.J.6    Del Sol, R.7
  • 19
    • 84867672506 scopus 로고    scopus 로고
    • The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement
    • K.H. Ebrahimi, E. Bill, P.L. Hagedoorn, and W.R. Hagen The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement Nat. Chem. Biol. 8 2012 941 948
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 941-948
    • Ebrahimi, K.H.1    Bill, E.2    Hagedoorn, P.L.3    Hagen, W.R.4
  • 21
    • 6344256938 scopus 로고    scopus 로고
    • Seeing green bacteria in a new light: Genomics-enabled studies of the photosynthetic apparatus in green sulfur bacteria and filamentous anoxygenic phototrophic bacteria
    • N.U. Frigaard, and D.A. Bryant Seeing green bacteria in a new light: genomics-enabled studies of the photosynthetic apparatus in green sulfur bacteria and filamentous anoxygenic phototrophic bacteria Arch. Microbiol. 182 2004 265 276
    • (2004) Arch. Microbiol. , vol.182 , pp. 265-276
    • Frigaard, N.U.1    Bryant, D.A.2
  • 23
    • 78651289421 scopus 로고    scopus 로고
    • Cloning and characterization of Chlorobium tepidum ferritin
    • A.E. Yevenes, V. Marquez, and R.K. Watt Cloning and characterization of Chlorobium tepidum ferritin Biochimie 93 2011 352 360
    • (2011) Biochimie , vol.93 , pp. 352-360
    • Yevenes, A.E.1    Marquez, V.2    Watt, R.K.3
  • 29
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • M.S. Weiss Global indicators of X-ray data quality J. Appl. Crystallogr. 34 2001 130 135
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 130-135
    • Weiss, M.S.1
  • 34
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular dynamics
    • M. Tuckerman, B.J. Berne, and G.J. Martyn Reversible multiple time scale molecular dynamics J. Chem. Phys. 97 1992 1990 2001
    • (1992) J. Chem. Phys. , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyn, G.J.3
  • 36
    • 48749148224 scopus 로고
    • Rattle: A "velocity" version of the shake algorithm for molecular dynamics calculations
    • H.C. Andersen Rattle: a "velocity" version of the shake algorithm for molecular dynamics calculations J. Comp. Phys. 52 1983 24 34
    • (1983) J. Comp. Phys. , vol.52 , pp. 24-34
    • Andersen, H.C.1
  • 38
    • 16644386131 scopus 로고    scopus 로고
    • Impact of a Poisson-Boltzmann electrostatic restraint on protein structures refined at medium resolution
    • A. Korostelev, M.O. Fenley, and M.S. Chapman Impact of a Poisson-Boltzmann electrostatic restraint on protein structures refined at medium resolution Acta Crystallogr. D Biol. Crystallogr. 60 2004 1786 1794
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1786-1794
    • Korostelev, A.1    Fenley, M.O.2    Chapman, M.S.3
  • 40
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • N.A. Baker, D. Sept, S. Joseph, M.J. Holst, and J.A. McCammon Electrostatics of nanosystems: application to microtubules and the ribosome Proc. Natl. Acad. Sci. 98 2001 10037 10041
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 41
    • 51849139041 scopus 로고    scopus 로고
    • Alignment of protein structures in the presence of domain motions
    • R. Mosca, B. Brannetti, and T.R. Schneider Alignment of protein structures in the presence of domain motions BMC Bioinform. 9 2008 352
    • (2008) BMC Bioinform. , vol.9 , pp. 352
    • Mosca, R.1    Brannetti, B.2    Schneider, T.R.3
  • 44
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • P. Arosio, R. Ingrassia, and P. Cavadini Ferritins: a family of molecules for iron storage, antioxidation and more Biochim. Biophys. Acta 1790 2009 589 599
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 45
    • 0034614666 scopus 로고    scopus 로고
    • A short Fe-Fe distance in peroxodiferric ferritin: Control of Fe substrate versus cofactor decay?
    • J. Hwang, C. Krebs, B.H. Huynh, D.E. Edmondson, E.C. Theil, and J.E. Penner-Hahn A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science 287 2000 122 125
    • (2000) Science , vol.287 , pp. 122-125
    • Hwang, J.1    Krebs, C.2    Huynh, B.H.3    Edmondson, D.E.4    Theil, E.C.5    Penner-Hahn, J.E.6
  • 46
    • 0026535851 scopus 로고
    • Mechanism of catalysis of Fe(II) oxidation by ferritin H chains
    • A. Treffry, J. Hirzmann, S.J. Yewdall, and P.M. Harrison Mechanism of catalysis of Fe(II) oxidation by ferritin H chains FEBS Lett. 302 1992 108 112
    • (1992) FEBS Lett. , vol.302 , pp. 108-112
    • Treffry, A.1    Hirzmann, J.2    Yewdall, S.J.3    Harrison, P.M.4
  • 49
    • 84902864885 scopus 로고    scopus 로고
    • The C-terminal regions have an important role in the activity of the ferroxidase center and the stability of Chlorobium tepidum ferritin
    • C. Brito, C. Matias, F.D. Gonzalez-Nilo, R.K. Watt, and A. Yévenes The C-terminal regions have an important role in the activity of the ferroxidase center and the stability of Chlorobium tepidum ferritin Protein J. 33 2014 211 220
    • (2014) Protein J. , vol.33 , pp. 211-220
    • Brito, C.1    Matias, C.2    Gonzalez-Nilo, F.D.3    Watt, R.K.4    Yévenes, A.5


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