메뉴 건너뛰기




Volumn 376, Issue 1, 2003, Pages 35-41

Oxo-iron clusters in a bacterial iron-trafficking protein: New roles for a conserved motif

Author keywords

Bacterial transferrin; Dityrosyl motif; Iron transport; Iron binding protein; Oxo iron cluster; X ray crystallography

Indexed keywords

BACTERIA; CELLS; CRYSTAL STRUCTURE; INTERFACES (MATERIALS); IRON; PROTEINS; X RAY CRYSTALLOGRAPHY;

EID: 0345688126     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031283     Document Type: Article
Times cited : (37)

References (43)
  • 1
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond, K. N., Dertz, E. A. and Kim, S. S. (2003) Enterobactin: An archetype for microbial iron transport. Proc. Natl. Acad. Sci. U.S.A. 100, 3584-3588
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 4
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. and Dover, L. G. (2000) Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 54, 881-941
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 5
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun, V. and Braun, M. (2002) Active transport of iron and siderophore antibiotics. Curr. Opin. Microbiol. 5, 194-201
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 194-201
    • Braun, V.1    Braun, M.2
  • 6
    • 0037317173 scopus 로고    scopus 로고
    • Acquisition of siderophores in Gram-negative bacteria
    • Faraldo-Gomez, J. D. and Sansom, M. S. P. (2003) Acquisition of siderophores in Gram-negative bacteria. Nat. Rev. Mol. Cell Biol. 4, 105-116
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 105-116
    • Faraldo-Gomez, J.D.1    Sansom, M.S.P.2
  • 7
    • 0035907067 scopus 로고    scopus 로고
    • Bacterial recognition of mineral surfaces: Nanoscale interactions between Shewanella and α-Fe00H
    • Washington, D.C.
    • Lower, S. K., Hochella, Jr, M. F. and Beveridge, T. J. (2001) Bacterial recognition of mineral surfaces: nanoscale interactions between Shewanella and α-Fe00H. Science (Washington, D.C.) 292, 1360-1363
    • (2001) Science , vol.292 , pp. 1360-1363
    • Lower, S.K.1    Hochella Jr., M.F.2    Beveridge, T.J.3
  • 9
    • 0021240437 scopus 로고
    • Identification of an iron-regulated 37,000-Dalton protein in the cell envelope of Neisseria gonorrhoeae
    • Mietzner, T A., Luginbuhl, G. H., Sandstrom, E. and Morse, S. A. (1984) Identification of an iron-regulated 37,000-Dalton protein in the cell envelope of Neisseria gonorrhoeae. Infect. Immun. 45, 410-416
    • (1984) Infect. Immun. , vol.45 , pp. 410-416
    • Mietzner, T.A.1    Luginbuhl, G.H.2    Sandstrom, E.3    Morse, S.A.4
  • 10
    • 0031948656 scopus 로고    scopus 로고
    • A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth
    • Khun, H. H., Kirby, S. D. and Lee, B. C. (1998) A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66, 2330-2336
    • (1998) Infect. Immun. , vol.66 , pp. 2330-2336
    • Khun, H.H.1    Kirby, S.D.2    Lee, B.C.3
  • 15
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: Common structural principles in proteins that transport iron and heme
    • Baker, H. M., Anderson, B. F. and Baker, E. N. (2003) Dealing with iron: common structural principles in proteins that transport iron and heme. Proc. Natl. Acad. Sci. U.S.A. 100, 3579-3583
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 19
    • 33751157391 scopus 로고
    • Syntheses, structures, and magnetic properties of two dinuclear iron(III) citrate complexes
    • Shweky, I., Bino, A., Goldberg, D. P. and Lippard, S. J. (1994) Syntheses, structures, and magnetic properties of two dinuclear iron(III) citrate complexes. Inorg. Chem. 33, 5161-5162
    • (1994) Inorg. Chem. , vol.33 , pp. 5161-5162
    • Shweky, I.1    Bino, A.2    Goldberg, D.P.3    Lippard, S.J.4
  • 20
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 85081424140 scopus 로고    scopus 로고
    • Twinning in presence of multiple NCS: Metals in a bacterial transferrin
    • in press
    • Alexeev, D. (2003) Twinning in presence of multiple NCS: metals in a bacterial transferrin. Acta Crystallogr., Sect. D: Biol. Crystallogr., in press
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr.
    • Alexeev, D.1
  • 23
    • 0037169658 scopus 로고    scopus 로고
    • Triisopropyltriazacyclononane copper(II): An efficient phosphodiester hydrolysis catalyst and DNA cleavage agent
    • Deck, K. M., Tseng, T. A. and Burstyn, J. N. (2002) Triisopropyltriazacyclononane copper(II): an efficient phosphodiester hydrolysis catalyst and DNA cleavage agent. Inorg. Chem. 41, 669-677
    • (2002) Inorg. Chem. , vol.41 , pp. 669-677
    • Deck, K.M.1    Tseng, T.A.2    Burstyn, J.N.3
  • 25
    • 0000064566 scopus 로고    scopus 로고
    • A novel nonairon(III) citrate complex: A 'ferric triple-decker'
    • Bino, A., Shweky, I., Cohen, S., Bauminger, E. R. and Lippard, S. J. (1998) A novel nonairon(III) citrate complex: a 'ferric triple-decker'. Inorg. Chem. 37, 5168-5172
    • (1998) Inorg. Chem. , vol.37 , pp. 5168-5172
    • Bino, A.1    Shweky, I.2    Cohen, S.3    Bauminger, E.R.4    Lippard, S.J.5
  • 27
    • 0000758665 scopus 로고
    • Hydrolytic polymerization of ferric citrate. I. Chemistry of the polymer
    • Spiro, T. G., Pape, L. and Saltman, P. (1967) Hydrolytic polymerization of ferric citrate. I. Chemistry of the polymer. J. Am. Chem. Soc. 89, 5555-5559
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 5555-5559
    • Spiro, T.G.1    Pape, L.2    Saltman, P.3
  • 28
    • 0037837866 scopus 로고    scopus 로고
    • High resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzae
    • Shouldice, S. R., Dougan, D. R., Skene, R. J., Tari, L. W., McRee, D. E., Yu, R. and Schryvers, A. B. (2003) High resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzae. J. Biol. Chem. 278, 11513-11519
    • (2003) J. Biol. Chem. , vol.278 , pp. 11513-11519
    • Shouldice, S.R.1    Dougan, D.R.2    Skene, R.J.3    Tari, L.W.4    McRee, D.E.5    Yu, R.6    Schryvers, A.B.7
  • 29
    • 0033537826 scopus 로고    scopus 로고
    • Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe
    • Mizutani, K., Yamashita, H., Kurokawa, H., Mikami, B. and Hirose, M. (1999) Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe. J. Biol. Chem. 274, 10190-10194
    • (1999) J. Biol. Chem. , vol.274 , pp. 10190-10194
    • Mizutani, K.1    Yamashita, H.2    Kurokawa, H.3    Mikami, B.4    Hirose, M.5
  • 30
    • 0036014775 scopus 로고    scopus 로고
    • The mechanism of iron uptake by transferrins: The X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex
    • Kuser, P., Hall, D. R., Haw, M., Neu, M., Evans, R. W. and Lindley, P. F. (2002) The mechanism of iron uptake by transferrins: the X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex. Acta Crystallogr. D: Biol. Crystallogr. 58, 777-783
    • (2002) Acta Crystallogr. D: Biol. Crystallogr. , vol.58 , pp. 777-783
    • Kuser, P.1    Hall, D.R.2    Haw, M.3    Neu, M.4    Evans, R.W.5    Lindley, P.F.6
  • 33
    • 37049128024 scopus 로고
    • Reactivity of phosphate esters. Diester hydrolysis
    • Kirby, A. J. and Younas, M. (1970) Reactivity of phosphate esters. Diester hydrolysis. J. Chem. Soc. B 510-513
    • (1970) J. Chem. Soc. B , pp. 510-513
    • Kirby, A.J.1    Younas, M.2
  • 34
    • 33845280194 scopus 로고
    • Cobalt(III) complex promoted hydrolysis of phosphate diesters: Change in rate-determining step with change in phosphate diester reactivity
    • Chin, J. and Zou, X. (1988) Cobalt(III) complex promoted hydrolysis of phosphate diesters: change in rate-determining step with change in phosphate diester reactivity. J. Am. Chem. Soc. 10, 223-225
    • (1988) J. Am. Chem. Soc. , vol.10 , pp. 223-225
    • Chin, J.1    Zou, X.2
  • 35
    • 0037387230 scopus 로고    scopus 로고
    • Iron acquisition: Straight up and on the rocks?
    • Butler, A. (2003) Iron acquisition: straight up and on the rocks? Nat. Struct. Biol. 10, 240-241
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 240-241
    • Butler, A.1
  • 36
    • 12644273812 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in di-iron-oxo proteins
    • Kurtz, D. M. (1997) Structural similarity and functional diversity in di-iron-oxo proteins. J. Biol. Inorg. Chem. 2, 159-167
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 159-167
    • Kurtz, D.M.1
  • 37
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • Theil, E. C. (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Annu. Rev. Biochem. 56, 289-315
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 38
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • Chasteen, N. D. and Harrison, P. M. (1999) Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol. 126, 182-194
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 39
    • 0038670302 scopus 로고    scopus 로고
    • The interface between the biological and inorganic worlds: Iron-sulfur metalloclusters
    • Washington, D.C.
    • Rees, D. C. and Howard, J. B. (2003) The interface between the biological and inorganic worlds: iron-sulfur metalloclusters. Science (Washington, D.C.) 300, 929
    • (2003) Science , vol.300 , pp. 929
    • Rees, D.C.1    Howard, J.B.2
  • 41
    • 0037016446 scopus 로고    scopus 로고
    • Intracellular iron minerals in a dissimilatory iron-reducing bacterium
    • Washington, D.C.
    • Glasauer, S., Langley, S. and Beveridge, T. J. (2002) Intracellular iron minerals in a dissimilatory iron-reducing bacterium. Science (Washington, D.C.) 295, 117-119
    • (2002) Science , vol.295 , pp. 117-119
    • Glasauer, S.1    Langley, S.2    Beveridge, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.