메뉴 건너뛰기




Volumn 198, Issue 7, 2016, Pages 1066-1076

Functional determinants of metal ion transport and selectivity in paralogous cation diffusion facilitator transporters CzcD and MntE in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; CATION; CATION DIFFUSION FACILITATOR TRANSPORTER; CZCD PROTEIN; METAL ION; MNTE PROTEIN; UNCLASSIFIED DRUG; ZINC; ANTIPORTER; METAL; REPRESSOR PROTEIN;

EID: 84961141569     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00975-15     Document Type: Article
Times cited : (49)

References (53)
  • 1
    • 84924923567 scopus 로고    scopus 로고
    • Metal limitation and toxicity at the interface between host and pathogen
    • Becker KW, Skaar EP. 2014. Metal limitation and toxicity at the interface between host and pathogen. FEMS Microbiol Rev 38:1235-1249. http://dx.doi.org/10.1111/1574-6976.12087.
    • (2014) FEMS Microbiol Rev , vol.38 , pp. 1235-1249
    • Becker, K.W.1    Skaar, E.P.2
  • 2
    • 84946487767 scopus 로고    scopus 로고
    • Cellular sensing and transport of metal ions: implications in micronutrient homeostasis
    • Bird AJ. 2015. Cellular sensing and transport of metal ions: implications in micronutrient homeostasis. J Nutr Biochem 26:1103-1115. http://dx.doi.org/10.1016/j.jnutbio.2015.08.002.
    • (2015) J Nutr Biochem , vol.26 , pp. 1103-1115
    • Bird, A.J.1
  • 3
    • 80053303115 scopus 로고    scopus 로고
    • Hammering out details: regulating metal levels in eukaryotes
    • Ehrensberger KM, Bird AJ. 2011. Hammering out details: regulating metal levels in eukaryotes. Trends Biochem Sci 36:524-531. http://dx.doi.org/10.1016/j.tibs.2011.07.002.
    • (2011) Trends Biochem Sci , vol.36 , pp. 524-531
    • Ehrensberger, K.M.1    Bird, A.J.2
  • 4
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay JA, Chin SM, Linn S. 1988. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240: 640-642. http://dx.doi.org/10.1126/science.2834821.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 5
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase
    • Touati D, Jacques M, Tardat B, Bouchard L, Despied S. 1995. Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J Bacteriol 177:2305-2314.
    • (1995) J Bacteriol , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 6
    • 21544465580 scopus 로고    scopus 로고
    • Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hp mutants of Escherichia coli
    • Park S, You X, Imlay JA. 2005. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hp mutants of Escherichia coli. Proc Natl Acad SciUSA102:9317-9322. http://dx.doi.org/10.1073/pnas.0502051102.
    • (2005) Proc Natl Acad SciUSA , vol.102 , pp. 9317-9322
    • Park, S.1    You, X.2    Imlay, J.A.3
  • 7
    • 84907820812 scopus 로고    scopus 로고
    • The mismetallation of enzymes during oxidative stress
    • Imlay JA. 2014. The mismetallation of enzymes during oxidative stress. J Biol Chem 289:28121-28128. http://dx.doi.org/10.1074/jbc.R114.588814.
    • (2014) J Biol Chem , vol.289 , pp. 28121-28128
    • Imlay, J.A.1
  • 8
    • 84926292718 scopus 로고    scopus 로고
    • The Escherichia coli small protein MntS and exporter MntP optimize the intracellular concentration of manganese
    • Martin JE, Waters LS, Storz G, Imlay JA. 2015. The Escherichia coli small protein MntS and exporter MntP optimize the intracellular concentration of manganese. PLoS Genet 11:e1004977. http://dx.doi.org/10.1371/journal.pgen.1004977.
    • (2015) PLoS Genet , vol.11
    • Martin, J.E.1    Waters, L.S.2    Storz, G.3    Imlay, J.A.4
  • 9
    • 84887113673 scopus 로고    scopus 로고
    • Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae
    • Lisher JP, Higgins KA, Maroney MJ, Giedroc DP. 2013. Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae. Biochemistry 52:7689-7701. http://dx.doi.org/10.1021/bi401132w.
    • (2013) Biochemistry , vol.52 , pp. 7689-7701
    • Lisher, J.P.1    Higgins, K.A.2    Maroney, M.J.3    Giedroc, D.P.4
  • 10
    • 84879501095 scopus 로고    scopus 로고
    • Superoxide poisons mononuclear iron enzymes by causing mismetallation
    • Gu M, Imlay JA. 2013. Superoxide poisons mononuclear iron enzymes by causing mismetallation. Mol Microbiol 89:123-134. http://dx.doi.org/10.1111/mmi.12263.
    • (2013) Mol Microbiol , vol.89 , pp. 123-134
    • Gu, M.1    Imlay, J.A.2
  • 11
    • 84903362295 scopus 로고    scopus 로고
    • Extracellular zinc competitively inhibits manganese uptake and compromises oxidative stress management in Streptococcus pneumoniae
    • Eijkelkamp BA, Morey JR, Ween MP, Ong CL, McEwan AG, Paton JC, McDevitt CA. 2014. Extracellular zinc competitively inhibits manganese uptake and compromises oxidative stress management in Streptococcus pneumoniae. PLoS One 9:e89427. http://dx.doi.org/10.1371/journal.pone.0089427.
    • (2014) PLoS One , vol.9
    • Eijkelkamp, B.A.1    Morey, J.R.2    Ween, M.P.3    Ong, C.L.4    McEwan, A.G.5    Paton, J.C.6    McDevitt, C.A.7
  • 12
    • 80455163132 scopus 로고    scopus 로고
    • Cobalt stress in Escherichia coli and Salmonella enterica: molecular bases for toxicity and resistance
    • Barras F, Fontecave M. 2011. Cobalt stress in Escherichia coli and Salmonella enterica: molecular bases for toxicity and resistance. Metallomics 3:1130-1134. http://dx.doi.org/10.1039/c1mt00099c.
    • (2011) Metallomics , vol.3 , pp. 1130-1134
    • Barras, F.1    Fontecave, M.2
  • 13
    • 82155168222 scopus 로고    scopus 로고
    • Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli
    • Macomber L, Elsey SP, Hausinger RP. 2011. Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli. Mol Microbiol 82:1291-1300. http://dx.doi.org/10.1111/j.1365-2958.2011.07891.x.
    • (2011) Mol Microbiol , vol.82 , pp. 1291-1300
    • Macomber, L.1    Elsey, S.P.2    Hausinger, R.P.3
  • 14
    • 80455163148 scopus 로고    scopus 로고
    • Mechanisms of nickel toxicity in microorganisms
    • Macomber L, Hausinger RP. 2011. Mechanisms of nickel toxicity in microorganisms. Metallomics 3:1153-1162. http://dx.doi.org/10.1039/c1mt00063b.
    • (2011) Metallomics , vol.3 , pp. 1153-1162
    • Macomber, L.1    Hausinger, R.P.2
  • 15
    • 84861138966 scopus 로고    scopus 로고
    • Silver(I), mercury(II), cadmium(II), and zinc(II) target exposed enzymic iron-sulfur clusters when they toxify Escherichia coli
    • Xu FF, Imlay JA. 2012. Silver(I), mercury(II), cadmium(II), and zinc(II) target exposed enzymic iron-sulfur clusters when they toxify Escherichia coli. Appl Environ Microbiol 78:3614-3621. http://dx.doi.org/10.1128/AEM.07368-11.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3614-3621
    • Xu, F.F.1    Imlay, J.A.2
  • 16
    • 84876199009 scopus 로고    scopus 로고
    • Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu(+)-ATPase mutant copA( ) of Rubrivivax gelatinosus
    • Azzouzi A, Steunou AS, Durand A, Khalfaoui-Hassani B, Bourbon ML, Astier C, Bollivar DW, Ouchane S. 2013. Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu(+)-ATPase mutant copA( ) of Rubrivivax gelatinosus. Mol Microbiol 88:339-351. http://dx.doi.org/10.1111/mmi.12188.
    • (2013) Mol Microbiol , vol.88 , pp. 339-351
    • Azzouzi, A.1    Steunou, A.S.2    Durand, A.3    Khalfaoui-Hassani, B.4    Bourbon, M.L.5    Astier, C.6    Bollivar, D.W.7    Ouchane, S.8
  • 17
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber L, Imlay JA. 2009. The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc Natl Acad Sci U S A 106:8344-8349. http://dx.doi.org/10.1073/pnas.0812808106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 18
    • 84937763688 scopus 로고    scopus 로고
    • Cation diffusion facilitator family: structure and function
    • Kolaj-Robin O, Russell D, Hayes KA, Pembroke JT, Soulimane T. 2015. Cation diffusion facilitator family: structure and function. FEBS Lett 589: 1283-1295. http://dx.doi.org/10.1016/j.febslet.2015.04.007.
    • (2015) FEBS Lett , vol.589 , pp. 1283-1295
    • Kolaj-Robin, O.1    Russell, D.2    Hayes, K.A.3    Pembroke, J.T.4    Soulimane, T.5
  • 20
    • 84907608789 scopus 로고    scopus 로고
    • The cation diffusion facilitator protein EmfA of Rhizobium etli belongs to a novel subfamily of Mn(2+)/Fe(2+) transporters conserved in alpha-proteobacteria
    • Cubillas C, Vinuesa P, Tabche ML, Davalos A, Vazquez A, Hernandez-Lucas I, Romero D, Garcia-de los Santos A. 2014. The cation diffusion facilitator protein EmfA of Rhizobium etli belongs to a novel subfamily of Mn(2+)/Fe(2+) transporters conserved in alpha-proteobacteria. Metallomics 6:1808-1815. http://dx.doi.org/10.1039/C4MT00135D.
    • (2014) Metallomics , vol.6 , pp. 1808-1815
    • Cubillas, C.1    Vinuesa, P.2    Tabche, M.L.3    Davalos, A.4    Vazquez, A.5    Hernandez-Lucas, I.6    Romero, D.7    Garcia-de los Santos, A.8
  • 21
    • 62949119234 scopus 로고    scopus 로고
    • Role of the manganese efflux system mntE for signalling and pathogenesis in Streptococcus pneumoniae
    • Rosch JW, Gao G, Ridout G, Wang YD, Tuomanen EI. 2009. Role of the manganese efflux system mntE for signalling and pathogenesis in Streptococcus pneumoniae. Mol Microbiol 72:12-25. http://dx.doi.org/10.1111/j.1365-2958.2009.06638.x.
    • (2009) Mol Microbiol , vol.72 , pp. 12-25
    • Rosch, J.W.1    Gao, G.2    Ridout, G.3    Wang, Y.D.4    Tuomanen, E.I.5
  • 22
    • 84928802405 scopus 로고    scopus 로고
    • Manganese homeostasis in group A Streptococcus is critical for resistance to oxidative stress and virulence
    • Turner AG, Ong CL, Gillen CM, Davies MR, West NP, McEwan AG, Walker MJ. 2015. Manganese homeostasis in group A Streptococcus is critical for resistance to oxidative stress and virulence. mBio 6:e00278-15. http://dx.doi.org/10.1128/mBio.00278-15.
    • (2015) mBio , vol.6
    • Turner, A.G.1    Ong, C.L.2    Gillen, C.M.3    Davies, M.R.4    West, N.P.5    McEwan, A.G.6    Walker, M.J.7
  • 23
    • 12444299959 scopus 로고    scopus 로고
    • FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress
    • Grass G, Otto M, Fricke B, Haney CJ, Rensing C, Nies DH, Munkelt D. 2005. FieF (YiiP) from Escherichia coli mediates decreased cellular accumulation of iron and relieves iron stress. Arch Microbiol 183:9-18. http://dx.doi.org/10.1007/s00203-004-0739-4.
    • (2005) Arch Microbiol , vol.183 , pp. 9-18
    • Grass, G.1    Otto, M.2    Fricke, B.3    Haney, C.J.4    Rensing, C.5    Nies, D.H.6    Munkelt, D.7
  • 24
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • Lu M, Fu D. 2007. Structure of the zinc transporter YiiP. Science 317: 1746-1748. http://dx.doi.org/10.1126/science.1143748.
    • (2007) Science , vol.317 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 25
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu M, Chai J, Fu D. 2009. Structural basis for autoregulation of the zinc transporter YiiP. Nat Struct Mol Biol 16:1063-1067. http://dx.doi.org/10.1038/nsmb.1662.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 30
    • 0036691789 scopus 로고    scopus 로고
    • Isolation of a novel Thermus thermophilus metal efflux protein that improves Escherichia coli growth under stress conditions
    • Spada S, Pembroke JT, Wall JG. 2002. Isolation of a novel Thermus thermophilus metal efflux protein that improves Escherichia coli growth under stress conditions. Extremophiles 6:301-308. http://dx.doi.org/10.1007/s00792-001-0257-0.
    • (2002) Extremophiles , vol.6 , pp. 301-308
    • Spada, S.1    Pembroke, J.T.2    Wall, J.G.3
  • 31
    • 0344578041 scopus 로고    scopus 로고
    • CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34
    • Anton A, Grosse C, Reissmann J, Pribyl T, Nies DH. 1999. CzcD is a heavy metal ion transporter involved in regulation of heavy metal resistance in Ralstonia sp. strain CH34. J Bacteriol 181:6876-6881.
    • (1999) J Bacteriol , vol.181 , pp. 6876-6881
    • Anton, A.1    Grosse, C.2    Reissmann, J.3    Pribyl, T.4    Nies, D.H.5
  • 32
    • 0033037505 scopus 로고    scopus 로고
    • Chromosome-determined zincresponsible operon czr in Staphylococcus aureus strain 912
    • Kuroda M, Hayashi H, Ohta T. 1999. Chromosome-determined zincresponsible operon czr in Staphylococcus aureus strain 912. Microbiol Immunol 43:115-125. http://dx.doi.org/10.1111/j.1348-0421.1999.tb02382.x.
    • (1999) Microbiol Immunol , vol.43 , pp. 115-125
    • Kuroda, M.1    Hayashi, H.2    Ohta, T.3
  • 33
    • 78650014725 scopus 로고    scopus 로고
    • Identification and evaluation of the role of the manganese efflux protein in Deinococcus radiodurans
    • Sun H, Xu G, Zhan H, Chen H, Sun Z, Tian B, Hua Y. 2010. Identification and evaluation of the role of the manganese efflux protein in Deinococcus radiodurans. BMC Microbiol 10:319. http://dx.doi.org/10.1186/1471-2180-10-319.
    • (2010) BMC Microbiol , vol.10 , pp. 319
    • Sun, H.1    Xu, G.2    Zhan, H.3    Chen, H.4    Sun, Z.5    Tian, B.6    Hua, Y.7
  • 34
    • 78651311318 scopus 로고    scopus 로고
    • Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae
    • Jacobsen FE, Kazmierczak KM, Lisher JP, Winkler ME, Giedroc DP. 2011. Interplay between manganese and zinc homeostasis in the human pathogen Streptococcus pneumoniae. Metallomics 3:38-41. http://dx.doi.org/10.1039/C0MT00050G.
    • (2011) Metallomics , vol.3 , pp. 38-41
    • Jacobsen, F.E.1    Kazmierczak, K.M.2    Lisher, J.P.3    Winkler, M.E.4    Giedroc, D.P.5
  • 36
    • 26644450950 scopus 로고    scopus 로고
    • Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF)
    • Wei Y, Fu D. 2005. Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF). J Biol Chem 280:33716-33724. http://dx.doi.org/10.1074/jbc.M506107200.
    • (2005) J Biol Chem , vol.280 , pp. 33716-33724
    • Wei, Y.1    Fu, D.2
  • 37
    • 0035512266 scopus 로고    scopus 로고
    • An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneumoniae
    • Sung CK, Li H, Claverys JP, Morrison DA. 2001. An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneumoniae. Appl Environ Microbiol 67:5190-5196. http://dx.doi.org/10.1128/AEM.67.11.5190-5196.2001.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5190-5196
    • Sung, C.K.1    Li, H.2    Claverys, J.P.3    Morrison, D.A.4
  • 38
    • 80855144209 scopus 로고    scopus 로고
    • The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly
    • Uebe R, Junge K, Henn V, Poxleitner G, Katzmann E, Plitzko JM, Zarivach R, Kasama T, Wanner G, Posfai M, Bottger L, Matzanke B, Schuler D. 2011. The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol Microbiol 82:818-835. http://dx.doi.org/10.1111/j.1365-2958.2011.07863.x.
    • (2011) Mol Microbiol , vol.82 , pp. 818-835
    • Uebe, R.1    Junge, K.2    Henn, V.3    Poxleitner, G.4    Katzmann, E.5    Plitzko, J.M.6    Zarivach, R.7    Kasama, T.8    Wanner, G.9    Posfai, M.10    Bottger, L.11    Matzanke, B.12    Schuler, D.13
  • 39
    • 0027491241 scopus 로고
    • The ferric ironbinding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin
    • Chen CY, Berish SA, Morse SA, Mietzner TA. 1993. The ferric ironbinding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol Microbiol 10:311-318. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01957.x.
    • (1993) Mol Microbiol , vol.10 , pp. 311-318
    • Chen, C.Y.1    Berish, S.A.2    Morse, S.A.3    Mietzner, T.A.4
  • 40
    • 0028073139 scopus 로고
    • Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins
    • Nowalk AJ, Tencza SB, Mietzner TA. 1994. Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins. Biochemistry 33:12769-12775. http://dx.doi.org/10.1021/bi00209a007.
    • (1994) Biochemistry , vol.33 , pp. 12769-12775
    • Nowalk, A.J.1    Tencza, S.B.2    Mietzner, T.A.3
  • 41
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW. 2000. The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Biol 7:287-291. http://dx.doi.org/10.1038/74048.
    • (2000) Nat Struct Biol , vol.7 , pp. 287-291
    • Clarke, T.E.1    Ku, S.Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 42
    • 84885131955 scopus 로고    scopus 로고
    • Zinc coordination spheres in protein structures
    • Laitaoja M, Valjakka J, Janis J. 2013. Zinc coordination spheres in protein structures. Inorg Chem 52:10983-10991. http://dx.doi.org/10.1021/ic401072d.
    • (2013) Inorg Chem , vol.52 , pp. 10983-10991
    • Laitaoja, M.1    Valjakka, J.2    Janis, J.3
  • 43
    • 84908885748 scopus 로고    scopus 로고
    • Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport
    • Ehrnstorfer IA, Geertsma ER, Pardon E, Steyaert J, Dutzler R. 2014. Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat Struct Mol Biol 21:990-996. http://dx.doi.org/10.1038/nsmb.2904.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 990-996
    • Ehrnstorfer, I.A.1    Geertsma, E.R.2    Pardon, E.3    Steyaert, J.4    Dutzler, R.5
  • 44
    • 84895775033 scopus 로고    scopus 로고
    • Formiminoglutamase from Trypanosoma cruzi is an arginase-like manganese metalloenzyme
    • Hai Y, Dugery RJ, Healy D, Christianson DW. 2013. Formiminoglutamase from Trypanosoma cruzi is an arginase-like manganese metalloenzyme. Biochemistry 52:9294-9309. http://dx.doi.org/10.1021/bi401352h.
    • (2013) Biochemistry , vol.52 , pp. 9294-9309
    • Hai, Y.1    Dugery, R.J.2    Healy, D.3    Christianson, D.W.4
  • 47
    • 84873040007 scopus 로고    scopus 로고
    • K(+)-induced conformational changes in the trimeric betaine transporter BetP monitored by ATR-FTIR spectroscopy
    • Korkmaz F, Ressl S, Ziegler C, Mantele W. 2013. K(+)-induced conformational changes in the trimeric betaine transporter BetP monitored by ATR-FTIR spectroscopy. Biochim Biophys Acta 1828:1181-1191. http://dx.doi.org/10.1016/j.bbamem.2013.01.004.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 1181-1191
    • Korkmaz, F.1    Ressl, S.2    Ziegler, C.3    Mantele, W.4
  • 48
    • 61949479923 scopus 로고    scopus 로고
    • Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP
    • Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, Ziegler C. 2009. Molecular basis of transport and regulation in the Na(+)/betaine symporter BetP. Nature 458:47-52. http://dx.doi.org/10.1038/nature07819.
    • (2009) Nature , vol.458 , pp. 47-52
    • Ressl, S.1    Terwisscha van Scheltinga, A.C.2    Vonrhein, C.3    Ott, V.4    Ziegler, C.5
  • 50
    • 84907829274 scopus 로고    scopus 로고
    • Metal preferences and metallation
    • Foster AW, Osman D, Robinson NJ. 2014. Metal preferences and metallation. J Biol Chem 289:28095-28103. http://dx.doi.org/10.1074/jbc.R114.588145.
    • (2014) J Biol Chem , vol.289 , pp. 28095-28103
    • Foster, A.W.1    Osman, D.2    Robinson, N.J.3
  • 51
    • 34248649906 scopus 로고    scopus 로고
    • Phylogenetic and functional analysis of the cation diffusion facilitator (CDF) family: improved signature and prediction of substrate specificity
    • Montanini B, Blaudez D, Jeandroz S, Sanders D, Chalot M. 2007. Phylogenetic and functional analysis of the cation diffusion facilitator (CDF) family: improved signature and prediction of substrate specificity. BMC Genomics 8:107. http://dx.doi.org/10.1186/1471-2164-8-107.
    • (2007) BMC Genomics , vol.8 , pp. 107
    • Montanini, B.1    Blaudez, D.2    Jeandroz, S.3    Sanders, D.4    Chalot, M.5
  • 52
    • 84870551592 scopus 로고    scopus 로고
    • Evidence for zinc and cadmium binding in a CDF transporter lacking the cytoplasmic domain
    • Russell D, Soulimane T. 2012. Evidence for zinc and cadmium binding in a CDF transporter lacking the cytoplasmic domain. FEBS Lett 586:4332-4338. http://dx.doi.org/10.1016/j.febslet.2012.10.043.
    • (2012) FEBS Lett , vol.586 , pp. 4332-4338
    • Russell, D.1    Soulimane, T.2
  • 53
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert X, Gouet P. 2014. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res 42:W320-W324. http://dx.doi.org/10.1093/nar/gku316.
    • (2014) Nucleic Acids Res , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.