메뉴 건너뛰기




Volumn 194, Issue 23, 2012, Pages 6518-6526

Crystal structure of the Klebsiella pneumoniae NFeoB/FeoC complexand roles of feoc in regulation of fe2+ transport by the bacterialfeo system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; FEOB PROTEIN; FERROUS ION; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN FEOC; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84871048812     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01228-12     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. 2010. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66:213-221.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 2
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: building new software for automated crystallographic structure determination.
    • Adams PD, et al. 2002. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58:1948-1954.
    • (2002) Acta Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 3
    • 79961214373 scopus 로고    scopus 로고
    • The initiation of GTP hydrolysis by the G-domain of FeoB: insights from a transition-state complex structure
    • doi:10.1371/journal.pone.0023355
    • Ash MR, Maher M, Guss JM, Jormakka M. 2011. The initiation of GTP hydrolysis by the G-domain of FeoB: insights from a transition-state complex structure. PLoS One 6:e23355. doi:10.1371/journal.pone.0023355.
    • (2011) PLoS One , vol.6 , pp. 23355
    • Ash, M.R.1    Maher, M.2    Guss, J.M.3    Jormakka, M.4
  • 4
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger AT. 2007. Version 1.2 of the crystallography and NMR system. Nat. Protoc. 2:2728-2733.
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 6
    • 0032538276 scopus 로고    scopus 로고
    • The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeina (bullfrog)
    • Chang CF, et al. 1998. The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeina (bullfrog). J. Mol. Biol. 283:231-244.
    • (1998) J. Mol. Biol. , vol.283 , pp. 231-244
    • Chang, C.F.1
  • 8
    • 23044493465 scopus 로고    scopus 로고
    • A novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation
    • Dashper SG, et al. 2005. A novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation. J. Biol. Chem. 280:28095-28102.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28095-28102
    • Dashper, S.G.1
  • 9
    • 37449034071 scopus 로고    scopus 로고
    • Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB
    • Eng ET, Jalilian AR, Spasov KA, Unger VM. 2008. Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB. J. Mol. Biol. 375:1086-1097.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1086-1097
    • Eng, E.T.1    Jalilian, A.R.2    Spasov, K.A.3    Unger, V.M.4
  • 11
    • 69849110161 scopus 로고    scopus 로고
    • Structural basis of GDP release and gating in G protein coupled Fe2+ transport
    • Guilfoyle A, et al. 2009. Structural basis of GDP release and gating in G protein coupled Fe2+ transport. EMBO J. 28:2677-2685.
    • (2009) EMBO J. , vol.28 , pp. 2677-2685
    • Guilfoyle, A.1
  • 12
    • 0002369613 scopus 로고
    • Ferrous iron transport mutants in Escherichia coli K12
    • Hantke K. 1987. Ferrous iron transport mutants in Escherichia coli K12. FEMS Microbiol. Lett. 44:53-57.
    • (1987) FEMS Microbiol. Lett. , vol.44 , pp. 53-57
    • Hantke, K.1
  • 13
    • 70349775491 scopus 로고    scopus 로고
    • Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter
    • Hattori M, et al. 2009. Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter. Structure 17:1345-1355.
    • (2009) Structure , vol.17 , pp. 1345-1355
    • Hattori, M.1
  • 14
    • 77952582365 scopus 로고    scopus 로고
    • Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB
    • Hung KW, et al. 2010. Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB. J. Struct. Biol. 170:501-512.
    • (2010) J. Struct. Biol. , vol.170 , pp. 501-512
    • Hung, K.W.1
  • 15
    • 84865197337 scopus 로고    scopus 로고
    • NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
    • Hung KW, Juan TH, Hsu YL, Huang TH. 2012. NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae. J. Biomol. NMR 53:161-165.
    • (2012) J. Biomol. NMR , vol.53 , pp. 161-165
    • Hung, K.W.1    Juan, T.H.2    Hsu, Y.L.3    Huang, T.H.4
  • 16
  • 17
    • 0027487221 scopus 로고
    • Characterization of the ferrous iron uptake system of Escherichia coli
    • Kammler M, Schon C, Hantke K. 1993. Characterization of the ferrous iron uptake system of Escherichia coli. J. Bacteriol. 175:6212-6219.
    • (1993) J. Bacteriol. , vol.175 , pp. 6212-6219
    • Kammler, M.1    Schon, C.2    Hantke, K.3
  • 18
    • 84863816918 scopus 로고    scopus 로고
    • The FeoA protein is necessary for the FeoB transporter to import ferrous iron
    • Kim H, Lee H, Shin D. 2012. The FeoA protein is necessary for the FeoB transporter to import ferrous iron. Biochem. Biophys. Res. Commun. 423:733-738.
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , pp. 733-738
    • Kim, H.1    Lee, H.2    Shin, D.3
  • 19
    • 68949218299 scopus 로고    scopus 로고
    • Structure and function of the FeoB G-domain from Methanococcus jannaschii
    • Köster S, Wehner M, Herrmann C, Kühlbrandt W, Yildiz O. 2009. Structure and function of the FeoB G-domain from Methanococcus jannaschii. J. Mol. Biol. 392:405-419.
    • (2009) J. Mol. Biol. , vol.392 , pp. 405-419
    • Köster, S.1    Wehner, M.2    Herrmann, C.3    Kühlbrandt, W.4    Yildiz, O.5
  • 20
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 21
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acidsIUPAC-IUBMB-IUPAB Inter- Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • Markley JL, et al. 1998. Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter- Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. J. Biomol. NMR 12:1-23.
    • (1998) J. Biomol. NMR , vol.12 , pp. 1-23
    • Markley, J.L.1
  • 22
    • 0037059058 scopus 로고    scopus 로고
    • The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria
    • Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM. 2002. The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria. Proc. Natl. Acad. Sci. U. S. A. 99:16243-16248.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16243-16248
    • Marlovits, T.C.1    Haase, W.2    Herrmann, C.3    Aller, S.G.4    Unger, V.M.5
  • 23
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson A. 1990. Current approaches to macromolecular crystallization. Eur. J. Biochem. 189:1-23.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 1-23
    • Mcpherson, A.1
  • 24
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee DE. 1999. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • Mcree, D.E.1
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, 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
  • 26
    • 0031436026 scopus 로고    scopus 로고
    • Novel findings on the copper catalysed oxidation of cysteine
    • Pecci L, Montefoschi G, Musci Cavallini D. 1997. Novel findings on the copper catalysed oxidation of cysteine. Amino Acids 13:355-367.
    • (1997) Amino Acids , vol.13 , pp. 355-367
    • Pecci, L.1    Montefoschi, G.2    Cavallini, D.M.3
  • 27
    • 77649272520 scopus 로고    scopus 로고
    • Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila
    • Petermann N, Hansen G, Schmidt CL, Hilgenfeld R. 2010. Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila. FEBS Lett. 584:733-738.
    • (2010) FEBS Lett. , vol.584 , pp. 733-738
    • Petermann, N.1    Hansen, G.2    Schmidt, C.L.3    Hilgenfeld, R.4
  • 29
    • 0036785675 scopus 로고    scopus 로고
    • Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection
    • Robey M, Cianciotto NP. 2002. Legionella pneumophila feoAB promotes ferrous iron uptake and intracellular infection. Infect.Immun.70:5659-5669.
    • (2002) Infect.Immun , vol.70 , pp. 5659-5669
    • Robey, M.1    Cianciotto, N.P.2
  • 30
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: insights from structural analysis
    • Sprang SR. 1997. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66:639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 31
    • 34548443356 scopus 로고    scopus 로고
    • Structural basis of effector regulation and signal termination in heterotrimericGα proteins
    • Sprang SR, Chen Z, Du X. 2007. Structural basis of effector regulation and signal termination in heterotrimericGα proteins. Adv. Protein Chem. 74:1-65.
    • (2007) Adv. Protein Chem. , vol.74 , pp. 1-65
    • Sprang, S.R.1    Chen, Z.2    Du, X.3
  • 32
    • 0027394158 scopus 로고
    • Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine
    • Stojiljkovic I, Cobeljic M, Hantke K. 1993. Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine. FEMS Microbiol. Lett. 108:111.
    • (1993) FEMS Microbiol. Lett. , vol.108 , pp. 111
    • Stojiljkovic, I.1    Cobeljic, M.2    Hantke, K.3
  • 33
    • 30344457013 scopus 로고    scopus 로고
    • Solution structure of the DNA binding domain of the telomeric repeat-binding protein of Arabidopsis thaliana: a new fold with an additional C-terminal helix
    • Sue SC, et al. 2006. Solution structure of the DNA binding domain of the telomeric repeat-binding protein of Arabidopsis thaliana: a new fold with an additional C-terminal helix. J. Mol. Biol. 356:72-85.
    • (2006) J. Mol. Biol. , vol.356 , pp. 72-85
    • Sue, S.C.1
  • 34
    • 0029858954 scopus 로고    scopus 로고
    • Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse
    • Tsolis RM, Baumler AJ, Heffron F, Stojiljkovic I. 1996. Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse. Infect. Immun. 64:4549-4556.
    • (1996) Infect. Immun. , vol.64 , pp. 4549-4556
    • Tsolis, R.M.1    Baumler, A.J.2    Heffron, F.3    Stojiljkovic, I.4
  • 35
    • 0033913686 scopus 로고    scopus 로고
    • Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter
    • Velayudhan J, et al. 2000. Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter. Mol. Microbiol. 37:274-286.
    • (2000) Mol. Microbiol. , vol.37 , pp. 274-286
    • Velayudhan, J.1
  • 36
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step sitedirected and site-saturation mutagenesis protocol
    • doi:10.1093/nar/gnh110.
    • Zheng L, Baumann U, Reymond JL. 2004. An efficient one-step sitedirected and site-saturation mutagenesis protocol. Nucleic Acids Res. 32: e115. doi:10.1093/nar/gnh110.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 115
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.