메뉴 건너뛰기




Volumn 413, Issue 3, 2011, Pages 639-656

Structural characterization of intramolecular Hg2+ transfer between flexibly linked domains of mercuric ion reductase

Author keywords

intramolecular metal ion transfer; mercury resistance; metal trafficking; SANS; SAXS

Indexed keywords

BACTERIAL ENZYME; HYBRID PROTEIN; MERCURY; MERCURY (II) REDUCTASE; METALLOCHAPERONE; MUTANT PROTEIN; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 80054695834     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.08.042     Document Type: Article
Times cited : (21)

References (83)
  • 1
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • DOI 10.1016/S0168-6445(03)00046-9
    • Barkay T., Miller S.M., and Summers A.O. Bacterial mercury resistance from atoms to ecosystems FEMS Microbiol. Rev. 27 2003 355 384 (Pubitemid 36700435)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.2-3 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 2
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • DOI 10.1126/science.1085049
    • Finney L.A., and O'Halloran T.V. Transition metal speciation in the cell: insights from the chemistry of metal ion receptors Science 300 2003 931 936 (Pubitemid 36548870)
    • (2003) Science , vol.300 , Issue.5621 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 3
    • 0029792315 scopus 로고    scopus 로고
    • Bacterial heavy metal resistance: New surprises
    • DOI 10.1146/annurev.micro.50.1.753
    • Silver S., and Phung L.T. Bacterial heavy metal resistance: new surprises Annu. Rev. Microbiol. 50 1996 753 789 (Pubitemid 26337481)
    • (1996) Annual Review of Microbiology , vol.50 , pp. 753-789
    • Silver, S.1    Phung, L.T.2
  • 7
    • 0034913058 scopus 로고    scopus 로고
    • Function, structure, and mechanism of intracellular copper trafficking proteins
    • DOI 10.1146/annurev.biochem.70.1.677
    • Huffman D.L., and O'Halloran T.V. Function, structure, and mechanism of intracellular copper trafficking proteins Annu. Rev. Biochem. 70 2001 677 701 (Pubitemid 32662222)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 677-701
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 8
    • 59449093704 scopus 로고    scopus 로고
    • Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: Insights into the mechanism of methylmercury degradation
    • Lafrance-Vanasse J., Lefebvre M., Di Lello P., Sygusch J., and Omichinski J.G. Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation J. Biol. Chem. 284 2009 938 944
    • (2009) J. Biol. Chem. , vol.284 , pp. 938-944
    • Lafrance-Vanasse, J.1    Lefebvre, M.2    Di Lello, P.3    Sygusch, J.4    Omichinski, J.G.5
  • 9
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • DOI 10.1038/nsb0901-751
    • Lamb A.L., Torres A.S., O'Halloran T.V., and Rosenzweig A.C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone Nat. Struct. Biol. 8 2001 751 755 (Pubitemid 32803590)
    • (2001) Nature Structural Biology , vol.8 , Issue.9 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 13
    • 0034078827 scopus 로고    scopus 로고
    • Structure and chemistry of the copper chaperone proteins
    • DOI 10.1016/S1367-5931(99)00066-6
    • Rosenzweig A.C., and O'Halloran T.V. Structure and chemistry of the copper chaperone proteins Curr. Opin. Chem. Biol. 4 2000 140 147 (Pubitemid 30189303)
    • (2000) Current Opinion in Chemical Biology , vol.4 , Issue.2 , pp. 140-147
    • Rosenzweig, A.C.1    O'Halloran, T.V.2
  • 14
    • 0025882946 scopus 로고
    • Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607
    • Schiering N., Kabsch W., Moore M.J., Distefano M.D., Walsh C.T., and Pai E.F. Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607 Nature 352 1991 168 172 (Pubitemid 21896723)
    • (1991) Nature , vol.352 , Issue.6331 , pp. 168-172
    • Schiering, N.1    Kabsch, W.2    Moore, M.J.3    Distefano, M.D.4    Walsh, C.T.5    Pai, E.F.6
  • 15
    • 0030971055 scopus 로고    scopus 로고
    • Structures of the reduced and mercury-bound forms of merP, the periplasmic protein from the bacterial mercury detoxification system
    • DOI 10.1021/bi9631632
    • Steele R.A., and Opella S.J. Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system Biochemistry 36 1997 6885 6895 (Pubitemid 27258100)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 6885-6895
    • Steele, R.A.1    Opella, S.J.2
  • 16
    • 70349558132 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion protein CusB from Escherichia coli
    • Su C.C., Yang F., Long F., Reyon D., Routh M.D., and Kuo D.W. Crystal structure of the membrane fusion protein CusB from Escherichia coli J. Mol. Biol. 393 2009 342 355
    • (2009) J. Mol. Biol. , vol.393 , pp. 342-355
    • Su, C.C.1    Yang, F.2    Long, F.3    Reyon, D.4    Routh, M.D.5    Kuo, D.W.6
  • 17
    • 0036175362 scopus 로고    scopus 로고
    • Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures
    • DOI 10.1101/gr.196802
    • Arnesano F., Banci L., Bertini I., Ciofi-Baffoni S., Molteni E., Huffman D.L., and O'Halloran T.V. Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures Genome Res. 12 2002 255 271 (Pubitemid 34162992)
    • (2002) Genome Research , vol.12 , Issue.2 , pp. 255-271
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Ciofi-Baffoni, S.4    Molteni, E.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 18
    • 0036431502 scopus 로고    scopus 로고
    • A new zinc-protein coordination site in intracellular metal trafficking: Solution structure of the Apo and Zn(II) forms of ZntA(46-118)
    • DOI 10.1016/S0022-2836(02)01007-0
    • Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., and O'Halloran T.V. A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118) J. Mol. Biol. 323 2002 883 897 (Pubitemid 35341062)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.5 , pp. 883-897
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Finney, L.A.4    Outten, C.E.5    O'Halloran, T.V.6
  • 20
    • 0037035530 scopus 로고    scopus 로고
    • Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: Metal coordination environments and protein interactions
    • DOI 10.1021/bi025515c
    • Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M., and Dameron C.T. Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions Biochemistry 41 2002 5822 5829 (Pubitemid 34462703)
    • (2002) Biochemistry , vol.41 , Issue.18 , pp. 5822-5829
    • Cobine, P.A.1    George, G.N.2    Jones, C.E.3    Wickramasinghe, W.A.4    Solioz, M.5    Dameron, C.T.6
  • 22
    • 77956565971 scopus 로고    scopus 로고
    • Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gamma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione
    • Hong B., Nauss R., Harwood I.M., and Miller S.M. Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gamma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione Biochemistry 49 2010 8187 8196
    • (2010) Biochemistry , vol.49 , pp. 8187-8196
    • Hong, B.1    Nauss, R.2    Harwood, I.M.3    Miller, S.M.4
  • 23
    • 23744482969 scopus 로고    scopus 로고
    • Direct monitoring of metal ion transfer between two trafficking proteins
    • DOI 10.1021/ja052872c
    • Ledwidge R., Soinski R., and Miller S.M. Direct monitoring of metal ion transfer between two trafficking proteins J. Am. Chem. Soc. 127 2005 10842 10843 (Pubitemid 41129855)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.31 , pp. 10842-10843
    • Ledwidge, R.1    Soinski, R.2    Miller, S.M.3
  • 24
    • 68749097278 scopus 로고    scopus 로고
    • Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces
    • Banci L., Bertini I., Calderone V., Della-Malva N., Felli I.C., and Neri S. Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces Biochem. J. 422 2009 37 42
    • (2009) Biochem. J. , vol.422 , pp. 37-42
    • Banci, L.1    Bertini, I.2    Calderone, V.3    Della-Malva, N.4    Felli, I.C.5    Neri, S.6
  • 25
    • 66149157256 scopus 로고    scopus 로고
    • An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1
    • Banci L., Bertini I., Cantini F., Massagni C., Migliardi M., and Rosato A. An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1 J. Biol. Chem. 284 2009 9354 9360
    • (2009) J. Biol. Chem. , vol.284 , pp. 9354-9360
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Massagni, C.4    Migliardi, M.5    Rosato, A.6
  • 26
    • 78249274906 scopus 로고    scopus 로고
    • A thermophilic bacterial origin and subsequent constraints by redox, light and salinity on the evolution of the microbial mercuric reductase
    • Barkay T., Kritee K., Boyd E., and Geesey G. A thermophilic bacterial origin and subsequent constraints by redox, light and salinity on the evolution of the microbial mercuric reductase Environ. Microbiol. 12 2010 2904 2917
    • (2010) Environ. Microbiol. , vol.12 , pp. 2904-2917
    • Barkay, T.1    Kritee, K.2    Boyd, E.3    Geesey, G.4
  • 27
    • 0000918801 scopus 로고
    • Reactions between mercuric mercury and cysteine and glutathione. Apparent dissociation constants, heats and entropies of formation of various forms of mercuric mercapto-cysteine and -glutathione
    • Stricks W., and Kolthoff I.M. Reactions between mercuric mercury and cysteine and glutathione. Apparent dissociation constants, heats and entropies of formation of various forms of mercuric mercapto-cysteine and -glutathione J. Am. Chem. Soc. 75 1953 5673 5681
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 5673-5681
    • Stricks, W.1    Kolthoff, I.M.2
  • 29
    • 0026677369 scopus 로고
    • Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans
    • Sedlmeier R., and Altenbuchner J. Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans Mol. Gen. Genet. 236 1992 76 85 (Pubitemid 23000626)
    • (1992) Molecular and General Genetics , vol.236 , Issue.1 , pp. 76-85
    • Sedlmeier, R.1    Altenbuchner, J.2
  • 30
    • 0021106293 scopus 로고
    • Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase
    • Brown N.L., Ford S.J., Pridmore R.D., and Fritzinger D.C. Nucleotide sequence of a gene from the Pseudomonas transposon Tn501 encoding mercuric reductase Biochemistry 22 1983 4089 4095
    • (1983) Biochemistry , vol.22 , pp. 4089-4095
    • Brown, N.L.1    Ford, S.J.2    Pridmore, R.D.3    Fritzinger, D.C.4
  • 31
    • 0022439117 scopus 로고
    • Organization, expression, and evolution of genes for mercury resistance
    • Summers A.O. Organization, expression, and evolution of genes for mercury resistance Annu. Rev. Microbiol. 40 1986 607 634
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 607-634
    • Summers, A.O.1
  • 32
    • 0024573091 scopus 로고
    • Nucleotide sequence of a chromosomal mercury resistance determinant from a Bacillus sp. with broad-spectrum mercury resistance
    • Wang Y., Moore M., Levinson H.S., Silver S., Walsh C., and Mahler I. Nucleotide sequence of a chromosomal mercury resistance determinant from a Bacillus sp. with broad-spectrum mercury resistance J. Bacteriol. 171 1989 83 92
    • (1989) J. Bacteriol. , vol.171 , pp. 83-92
    • Wang, Y.1    Moore, M.2    Levinson, H.S.3    Silver, S.4    Walsh, C.5    Mahler, I.6
  • 33
    • 0024520558 scopus 로고
    • Mutagenesis of the redox-active disulfide in mercuric ion reductase: Catalysis by mutant enzymes restricted to flavin redox chemistry
    • DOI 10.1021/bi00429a035
    • Distefano M.D., Au K.G., and Walsh C.T. Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry Biochemistry 28 1989 1168 1183 (Pubitemid 19058691)
    • (1989) Biochemistry , vol.28 , Issue.3 , pp. 1168-1183
    • Distefano, M.D.1    Au, K.G.2    Walsh, C.T.3
  • 34
    • 0025271840 scopus 로고
    • 559 from the adjacent subunit: Evidence from in vivo and in vitro heterodimer formation
    • Distefano M.D., Moore M.J., and Walsh C.T. Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation Biochemistry 29 1990 2703 2713 (Pubitemid 20122604)
    • (1990) Biochemistry , vol.29 , Issue.11 , pp. 2703-2713
    • Distefano, M.D.1    Moore, M.J.2    Walsh, C.T.3
  • 35
    • 0033596895 scopus 로고    scopus 로고
    • 2 into the active site of mercuric ion reductase depend on the nature of the X ligands
    • 2 into the active site of mercuric ion reductase depend on the nature of the X ligands Biochemistry 38 1999 3519 3529
    • (1999) Biochemistry , vol.38 , pp. 3519-3529
    • Engst, S.1    Miller, S.M.2
  • 36
    • 0021106272 scopus 로고
    • Mercuric reductase: Homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide
    • Fox B.S., and Walsh C.T. Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide Biochemistry 22 1983 4082 4088
    • (1983) Biochemistry , vol.22 , pp. 4082-4088
    • Fox, B.S.1    Walsh, C.T.2
  • 38
    • 0024583558 scopus 로고
    • Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: Consequences for bacterial detoxification of mercurials
    • DOI 10.1021/bi00429a036
    • Moore M.J., and Walsh C.T. Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: consequences for bacterial detoxification of mercurials Biochemistry 28 1989 1183 1194 (Pubitemid 19058692)
    • (1989) Biochemistry , vol.28 , Issue.3 , pp. 1183-1194
    • Moore, M.J.1    Walsh, C.T.2
  • 40
    • 0016385572 scopus 로고
    • Interaction between an R factor and an element conferring resistance to mercuric ions in Pseudomonas aeruginosa
    • Stanisich V.A. Interaction between an R factor and an element conferring resistance to mercuric ions in Pseudomonas aeruginosa Mol. Gen. Genet. 128 1974 201 212
    • (1974) Mol. Gen. Genet. , vol.128 , pp. 201-212
    • Stanisich, V.A.1
  • 41
    • 0017737414 scopus 로고
    • Characterization of a translocation unit encoding resistance to mercuric ions that occurs on a nonconjugative plasmid in Pseudomonas aeruginosa
    • Stanisich V.A., Bennett P.M., and Richmond M.H. Characterization of a translocation unit encoding resistance to mercuric ions that occurs on a nonconjugative plasmid in Pseudomonas aeruginosa J. Bacteriol. 129 1977 1227 1233 (Pubitemid 8109658)
    • (1977) Journal of Bacteriology , vol.129 , Issue.3 , pp. 1227-1233
    • Stanisich, V.A.1    Bennett, P.M.2    Richmond, M.H.3
  • 42
    • 78149459696 scopus 로고    scopus 로고
    • XLF regulates filament architecture of the XRCC4•ligase IV complex
    • Hammel M., Yu Y., Fang S., Lees-Miller S.P., and Tainer J.A. XLF regulates filament architecture of the XRCC4•ligase IV complex Structure 18 2010 1431 1442
    • (2010) Structure , vol.18 , pp. 1431-1442
    • Hammel, M.1    Yu, Y.2    Fang, S.3    Lees-Miller, S.P.4    Tainer, J.A.5
  • 43
    • 38549146411 scopus 로고    scopus 로고
    • Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering
    • Bernado P., Perez Y., Svergun D.I., and Pons M. Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering J. Mol. Biol. 376 2008 492 505
    • (2008) J. Mol. Biol. , vol.376 , pp. 492-505
    • Bernado, P.1    Perez, Y.2    Svergun, D.I.3    Pons, M.4
  • 45
    • 77950418698 scopus 로고    scopus 로고
    • Structural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scattering
    • Pretto D.I., Tsutakawa S., Brosey C.A., Castillo A., Chagot M.E., and Smith J.A. Structural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scattering Biochemistry 49 2010 2880 2889
    • (2010) Biochemistry , vol.49 , pp. 2880-2889
    • Pretto, D.I.1    Tsutakawa, S.2    Brosey, C.A.3    Castillo, A.4    Chagot, M.E.5    Smith, J.A.6
  • 47
    • 48449094112 scopus 로고    scopus 로고
    • Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles
    • Chaudhury S., and Gray J.J. Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles J. Mol. Biol. 381 2008 1068 1087
    • (2008) J. Mol. Biol. , vol.381 , pp. 1068-1087
    • Chaudhury, S.1    Gray, J.J.2
  • 48
    • 69849103777 scopus 로고    scopus 로고
    • Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
    • Jensen M.R., Markwick P.R., Meier S., Griesinger C., Zweckstetter M., and Grzesiek S. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings Structure 17 2009 1169 1185
    • (2009) Structure , vol.17 , pp. 1169-1185
    • Jensen, M.R.1    Markwick, P.R.2    Meier, S.3    Griesinger, C.4    Zweckstetter, M.5    Grzesiek, S.6
  • 49
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore G.M., and Iwahara J. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes Chem. Rev. 109 2009 4108 4139
    • (2009) Chem. Rev. , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 50
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • Rozycki B., Kim Y.C., and Hummer G. SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions Structure 19 2011 109 116
    • (2011) Structure , vol.19 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 52
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • Pelikan M., Hura G.L., and Hammel M. Structure and flexibility within proteins as identified through small angle X-ray scattering Gen. Physiol. Biophys. 28 2009 174 189
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 54
    • 78149258244 scopus 로고    scopus 로고
    • Proteins at work: A combined small angle x-ray scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape
    • Jamros M.A., Oliveira L.C., Whitford P.C., Onuchic J.N., Adams J.A., Blumenthal D.K., and Jennings P.A. Proteins at work: a combined small angle x-ray scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape J. Biol. Chem. 285 2010 36121 36128
    • (2010) J. Biol. Chem. , vol.285 , pp. 36121-36128
    • Jamros, M.A.1    Oliveira, L.C.2    Whitford, P.C.3    Onuchic, J.N.4    Adams, J.A.5    Blumenthal, D.K.6    Jennings, P.A.7
  • 55
    • 77951913268 scopus 로고    scopus 로고
    • Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II)
    • Guo H.B., Johs A., Parks J.M., Olliff L., Miller S.M., and Summers A.O. Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II) J. Mol. Biol. 398 2010 555 568
    • (2010) J. Mol. Biol. , vol.398 , pp. 555-568
    • Guo, H.B.1    Johs, A.2    Parks, J.M.3    Olliff, L.4    Miller, S.M.5    Summers, A.O.6
  • 56
    • 0020478725 scopus 로고
    • Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide
    • Fox B., and Walsh C.T. Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidation-reduction-active disulfide J. Biol. Chem. 257 1982 2498 2503
    • (1982) J. Biol. Chem. , vol.257 , pp. 2498-2503
    • Fox, B.1    Walsh, C.T.2
  • 57
    • 0021103439 scopus 로고
    • Mercuric reductase from R-plasmid NR1: Characterization and mechanistic study
    • Rinderle S.J., Booth J.E., and Williams J.W. Mercuric reductase from R-plasmid NR1: characterization and mechanistic study Biochemistry 22 1983 869 876
    • (1983) Biochemistry , vol.22 , pp. 869-876
    • Rinderle, S.J.1    Booth, J.E.2    Williams, J.W.3
  • 58
    • 0017806138 scopus 로고
    • The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli
    • Schottel J.L. The mercuric and organomercurial detoxifying enzymes from a plasmid-bearing strain of Escherichia coli J. Biol. Chem. 253 1978 4341 4349 (Pubitemid 8384125)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.12 , pp. 4341-4349
    • Schottel, J.L.1
  • 59
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid) - a reexamination
    • DOI 10.1016/0003-2697(79)90792-9
    • Riddles P.W., Blakeley R.L., and Zerner B. Ellmans reagent: 5,5′-dithiobis(2-nitrobenzoic acid)-a reexamination Anal. Biochem. 94 1979 75 81 (Pubitemid 9170207)
    • (1979) Analytical Biochemistry , vol.94 , Issue.1 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 62
    • 0035798652 scopus 로고    scopus 로고
    • Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase
    • Arnesano F., Banci L., Bertini I., Cantini F., Ciofi-Baffoni S., Huffman D.L., and O'Halloran T.V. Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase J. Biol. Chem. 276 2001 41365 41376
    • (2001) J. Biol. Chem. , vol.276 , pp. 41365-41376
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 63
    • 11844264877 scopus 로고    scopus 로고
    • Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: Dose-related considerations and suppression by cryoprotectants
    • DOI 10.1107/S0909049504019272
    • Kuwamoto S., Akiyama S., and Fujisawa T. Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: dose-related considerations and suppression by cryoprotectants J. Synchrotron Radiat. 11 2004 462 468 (Pubitemid 40087585)
    • (2004) Journal of Synchrotron Radiation , vol.11 , Issue.6 , pp. 462-468
    • Kuwamoto, S.1    Akiyama, S.2    Fujisawa, T.3
  • 64
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas E., and Svergun D.I. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering J. Appl. Crystallogr. 40 2007 S245 S249
    • (2007) J. Appl. Crystallogr. , vol.40
    • Mylonas, E.1    Svergun, D.I.2
  • 65
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny D., Hammel M., and Sali A. FoXS: a web server for rapid computation and fitting of SAXS profiles Nucleic Acids Res. 38 2010 W540 W544
    • (2010) Nucleic Acids Res. , vol.38
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 66
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503 (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 67
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam C.D., Hammel M., Hura G.L., and Tainer J.A. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution Q. Rev. Biophys. 40 2007 191 285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 71
    • 0022353698 scopus 로고
    • Versatile mercury-resistant cloning and expression vectors
    • DOI 10.1016/0378-1119(85)90326-9
    • Gambill B.D., and Summers A.O. Versatile mercury-resistant cloning and expression vectors Gene 39 1985 293 297 (Pubitemid 16175761)
    • (1985) Gene , vol.39 , Issue.2-3 , pp. 293-297
    • Gambill, B.D.1    Summers, A.O.2
  • 72
    • 0034996241 scopus 로고    scopus 로고
    • MBP fusion protein with a viral protease cleavage site: One-step cleavage/purification of insoluble proteins
    • Alexandrov A., Dutta K., and Pascal S.M. MBP fusion protein with a viral protease cleavage site: one-step cleavage/purification of insoluble proteins BioTechniques 30 2001 1194 1198 (Pubitemid 32523820)
    • (2001) BioTechniques , vol.30 , Issue.6 , pp. 1194-1198
    • Alexandrov, A.1    Dutta, K.2    Pascal, S.M.3
  • 73
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • DOI 10.1006/jmbi.1996.0399
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298 (Pubitemid 26254109)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.3 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 74
    • 77953562742 scopus 로고    scopus 로고
    • Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry
    • Johs A., Shi L., Droubay T., Ankner J.F., and Liang L. Characterization of the decaheme c-type cytochrome OmcA in solution and on hematite surfaces by small angle x-ray scattering and neutron reflectometry Biophys. J. 98 2010 3035 3043
    • (2010) Biophys. J. , vol.98 , pp. 3035-3043
    • Johs, A.1    Shi, L.2    Droubay, T.3    Ankner, J.F.4    Liang, L.5
  • 79
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 81
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • DOI 10.1110/ps.062416606
    • Shen M.Y., and Sali A. Statistical potential for assessment and prediction of protein structures Protein Sci. 15 2006 2507 2524 (Pubitemid 44771688)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.