메뉴 건너뛰기




Volumn 51, Issue 12, 2012, Pages 2619-2629

Solution structure of Mycobacterium tuberculosis NmtR in the apo state: Insights into Ni(II)-mediated allostery

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERY; AMIDINATION; AMINO GROUP; APO-STATE; DNA BINDING; DYNAMIC DISORDER; HEXACOORDINATION; METAL SENSING; MICROENVIRONMENTS; MOLECULAR DYNAMICS SIMULATIONS; MYCOBACTERIUM TUBERCULOSIS; N-TERMINALS; NI COMPLEXES; OPEN CONFORMATION; QUANTUM CHEMICAL CALCULATIONS; RATIOMETRIC; REGULATORY PROTEIN; SOLUTION STRUCTURES; STAPHYLOCOCCUS AUREUS; TIME-SCALES; ZN COMPLEX;

EID: 84859192888     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3001402     Document Type: Article
Times cited : (36)

References (78)
  • 2
    • 65949110356 scopus 로고    scopus 로고
    • Cooperative metal binding and helical folding in model peptides of treble-clef zinc fingers
    • Seneque, O., Bonnet, E., Joumas, F. L., and Latour, J. M. (2009) Cooperative metal binding and helical folding in model peptides of treble-clef zinc fingers Chemistry 15, 4798-4810
    • (2009) Chemistry , vol.15 , pp. 4798-4810
    • Seneque, O.1    Bonnet, E.2    Joumas, F.L.3    Latour, J.M.4
  • 3
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D. S. (2001) Zinc coordination sphere in biochemical zinc sites BioMetals 14, 271-313
    • (2001) BioMetals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 4
    • 34547229278 scopus 로고    scopus 로고
    • Metal sensor proteins: Nature's metalloregulated allosteric switches
    • Giedroc, D. P. and Arunkumar, A. I. (2007) Metal sensor proteins: Nature's metalloregulated allosteric switches Dalton Trans. 29, 3107-3120
    • (2007) Dalton Trans. , vol.29 , pp. 3107-3120
    • Giedroc, D.P.1    Arunkumar, A.I.2
  • 5
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma, Z., Jacobsen, F. E., and Giedroc, D. P. (2009) Coordination chemistry of bacterial metal transport and sensing Chem. Rev. 109, 4644-4681
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 6
    • 79956065205 scopus 로고    scopus 로고
    • Metalloregulatory proteins: Metal selectivity and allosteric switching
    • Reyes-Caballero, H., Campanello, G. C., and Giedroc, D. P. (2011) Metalloregulatory proteins: Metal selectivity and allosteric switching Biophys. Chem. 156, 103-114
    • (2011) Biophys. Chem. , vol.156 , pp. 103-114
    • Reyes-Caballero, H.1    Campanello, G.C.2    Giedroc, D.P.3
  • 7
    • 43049120578 scopus 로고    scopus 로고
    • Selective recognition of metal ions by metalloregulatory proteins
    • Chen, P. R. and He, C. (2008) Selective recognition of metal ions by metalloregulatory proteins Curr. Opin. Chem. Biol. 12, 214-221
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 214-221
    • Chen, P.R.1    He, C.2
  • 8
    • 33544471308 scopus 로고    scopus 로고
    • Metal ion transport and regulation in Mycobacterium tuberculosis
    • Agranoff, D. and Krishna, S. (2004) Metal ion transport and regulation in Mycobacterium tuberculosis Front. Biosci. 9, 2996-3006
    • (2004) Front. Biosci. , vol.9 , pp. 2996-3006
    • Agranoff, D.1    Krishna, S.2
  • 10
    • 0037565104 scopus 로고    scopus 로고
    • The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance
    • Busenlehner, L. S., Pennella, M. A., and Giedroc, D. P. (2003) The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance FEMS Microbiol. Rev. 27, 131-143
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 131-143
    • Busenlehner, L.S.1    Pennella, M.A.2    Giedroc, D.P.3
  • 12
    • 77952000337 scopus 로고    scopus 로고
    • Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors
    • Osman, D. and Cavet, J. S. (2010) Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors Nat. Prod. Rep. 27, 668-680
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 668-680
    • Osman, D.1    Cavet, J.S.2
  • 13
    • 79960423857 scopus 로고    scopus 로고
    • Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia
    • Guimaraes, B. G., Barbosa, R. L., Soprano, A. S., Campos, B. M., de Souza, T. A., Tonoli, C. C., Leme, A. F., Murakami, M. T., and Benedetti, C. E. (2011) Plant pathogenic bacteria utilize biofilm growth-associated repressor (BigR), a novel winged-helix redox switch, to control hydrogen sulfide detoxification under hypoxia J. Biol. Chem. 286, 26148-26157
    • (2011) J. Biol. Chem. , vol.286 , pp. 26148-26157
    • Guimaraes, B.G.1    Barbosa, R.L.2    Soprano, A.S.3    Campos, B.M.4    De Souza, T.A.5    Tonoli, C.C.6    Leme, A.F.7    Murakami, M.T.8    Benedetti, C.E.9
  • 15
    • 32044441204 scopus 로고    scopus 로고
    • Individual metal ligands play distinct functional roles in the zinc sensor Staphylococcus aureus CzrA
    • Pennella, M. A., Arunkumar, A. I., and Giedroc, D. P. (2006) Individual metal ligands play distinct functional roles in the zinc sensor Staphylococcus aureus CzrA J. Mol. Biol. 356, 1124-1136
    • (2006) J. Mol. Biol. , vol.356 , pp. 1124-1136
    • Pennella, M.A.1    Arunkumar, A.I.2    Giedroc, D.P.3
  • 16
    • 70849126660 scopus 로고    scopus 로고
    • Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state
    • Arunkumar, A. I., Campanello, G. C., and Giedroc, D. P. (2009) Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state Proc. Natl. Acad. Sci. U.S.A. 106, 18177-18182
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18177-18182
    • Arunkumar, A.I.1    Campanello, G.C.2    Giedroc, D.P.3
  • 17
    • 71749096822 scopus 로고    scopus 로고
    • Energetics of allosteric negative coupling in the zinc sensor S. aureus CzrA
    • Grossoehme, N. E. and Giedroc, D. P. (2009) Energetics of allosteric negative coupling in the zinc sensor S. aureus CzrA J. Am. Chem. Soc. 131, 17860-17870
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17860-17870
    • Grossoehme, N.E.1    Giedroc, D.P.2
  • 19
    • 0033037505 scopus 로고    scopus 로고
    • Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912
    • Kuroda, M., Hayashi, H., and Ohta, T. (1999) Chromosome-determined zinc-responsible operon czr in Staphylococcus aureus strain 912 Microbiol. Immunol. 43, 115-125
    • (1999) Microbiol. Immunol. , vol.43 , pp. 115-125
    • Kuroda, M.1    Hayashi, H.2    Ohta, T.3
  • 20
    • 0033009421 scopus 로고    scopus 로고
    • ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus
    • Singh, V. K., Xiong, A., Usgaard, T. R., Chakrabarti, S., Deora, R., Misra, T. K., and Jayaswal, R. K. (1999) ZntR is an autoregulatory protein and negatively regulates the chromosomal zinc resistance operon znt of Staphylococcus aureus Mol. Microbiol. 33, 200-207
    • (1999) Mol. Microbiol. , vol.33 , pp. 200-207
    • Singh, V.K.1    Xiong, A.2    Usgaard, T.R.3    Chakrabarti, S.4    Deora, R.5    Misra, T.K.6    Jayaswal, R.K.7
  • 23
    • 0036301096 scopus 로고    scopus 로고
    • Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: Evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins
    • Busenlehner, L. S., Weng, T. C., Penner-Hahn, J. E., and Giedroc, D. P. (2002) Elucidation of primary (α3N) and vestigial (α5) heavy metal-binding sites in Staphylococcus aureus pI258 CadC: Evolutionary implications for metal ion selectivity of ArsR/SmtB metal sensor proteins J. Mol. Biol. 319, 685-701
    • (2002) J. Mol. Biol. , vol.319 , pp. 685-701
    • Busenlehner, L.S.1    Weng, T.C.2    Penner-Hahn, J.E.3    Giedroc, D.P.4
  • 25
    • 0037064122 scopus 로고    scopus 로고
    • A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of cytosol and effector binding sites to metal selectivity
    • Cavet, J. S., Meng, W., Pennella, M. A., Appelhoff, R. J., Giedroc, D. P., and Robinson, N. J. (2002) A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of cytosol and effector binding sites to metal selectivity J. Biol. Chem. 277, 38441-38448
    • (2002) J. Biol. Chem. , vol.277 , pp. 38441-38448
    • Cavet, J.S.1    Meng, W.2    Pennella, M.A.3    Appelhoff, R.J.4    Giedroc, D.P.5    Robinson, N.J.6
  • 26
    • 80052742146 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR
    • Reyes-Caballero, H., Lee, C. W., and Giedroc, D. P. (2011) Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR Biochemistry 50, 7941-7952
    • (2011) Biochemistry , vol.50 , pp. 7941-7952
    • Reyes-Caballero, H.1    Lee, C.W.2    Giedroc, D.P.3
  • 27
    • 82555168079 scopus 로고    scopus 로고
    • Ratiometric pulse-chase amidination mass spectrometry as a probe of biomolecular complex formation
    • Chang, F. M., Lauber, M. A., Running, W. E., Reilly, J. P., and Giedroc, D. P. (2011) Ratiometric pulse-chase amidination mass spectrometry as a probe of biomolecular complex formation Anal. Chem. 83, 9092-9099
    • (2011) Anal. Chem. , vol.83 , pp. 9092-9099
    • Chang, F.M.1    Lauber, M.A.2    Running, W.E.3    Reilly, J.P.4    Giedroc, D.P.5
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 29
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Blevins, R. A. (1994) NMR View: A computer program for the visualization and analysis of NMR data J. Biomol. NMR 5, 603-614
    • (1994) J. Biomol. NMR , vol.5 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 31
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically- enriched proteins
    • Montelione, G. T., Lyons, B. A., Emerson, S. D., and Tashiro, M. (1992) An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins J. Am. Chem. Soc. 114, 10974-10975
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 34
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert, P. (2004) Automated NMR structure calculation with CYANA Methods Mol. Biol. 278, 353-378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 35
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Guntert, P., and Wuthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319, 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 36
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44, 213-223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 43
    • 0343614206 scopus 로고    scopus 로고
    • A systematic study of water models for molecular simulation: Derivation of water models optimized for use with a reaction field
    • van der Spoel, D., van Maaren, P. J., and Berendsen, H. J. C. (1998) A systematic study of water models for molecular simulation: Derivation of water models optimized for use with a reaction field J. Chem. Phys. 108, 10220-10230
    • (1998) J. Chem. Phys. , vol.108 , pp. 10220-10230
    • Van Der Spoel, D.1    Van Maaren, P.J.2    Berendsen, H.J.C.3
  • 44
    • 49449085241 scopus 로고    scopus 로고
    • Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations
    • Joung, I. S. and Cheatham, T. E., III (2008) Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations J. Phys. Chem. B 112, 9020-9041
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9020-9041
    • Joung, I.S.1    Cheatham III, T.E.2
  • 45
    • 36749113534 scopus 로고
    • Generalized Langevin equation approach for atom-solid-surface scattering: General formulation for classical scattering off harmonic solids
    • Adelman, S. A. and Doll, J. D. (1976) Generalized Langevin equation approach for atom-solid-surface scattering: General formulation for classical scattering off harmonic solids J. Chem. Phys. 64, 2375-2388
    • (1976) J. Chem. Phys. , vol.64 , pp. 2375-2388
    • Adelman, S.A.1    Doll, J.D.2
  • 46
    • 1542469206 scopus 로고
    • Generalized Langevin equation approach for atom-solid-surface scattering: Numerical techniques for Gaussian generalized Langevin dynamics
    • Doll, J. D. and Dion, D. R. (1976) Generalized Langevin equation approach for atom-solid-surface scattering: Numerical techniques for Gaussian generalized Langevin dynamics J. Chem. Phys. 65, 3762-3766
    • (1976) J. Chem. Phys. , vol.65 , pp. 3762-3766
    • Doll, J.D.1    Dion, D.R.2
  • 47
    • 36449007976 scopus 로고
    • The effect of long-range electrostatic interactions in simulations of macromolecular crystals: A comparison of the Ewald and truncated list methods
    • York, D. M., Darden, T. A., and Pedersen, L. G. (1993) The effect of long-range electrostatic interactions in simulations of macromolecular crystals: A comparison of the Ewald and truncated list methods J. Chem. Phys. 99, 8345-8348
    • (1993) J. Chem. Phys. , vol.99 , pp. 8345-8348
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3
  • 49
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM Methods for Biomolecular Systems
    • Senn, H. M. and Thiel, W. (2009) QM/MM Methods for Biomolecular Systems Angew. Chem. Int. Ed. 48, 1198-1229
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 50
    • 84859185149 scopus 로고    scopus 로고
    • version 5.7 () Schrödinger, New York.
    • Qsite, version 5.7 (2011) Schrödinger, New York.
    • (2011) Qsite
  • 51
    • 43049141516 scopus 로고    scopus 로고
    • The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: Two new functionals and systematic testing of four M06-class functionals and 12 other functionals
    • Zhao, Y. and Truhlar, D. G. (2008) The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: Two new functionals and systematic testing of four M06-class functionals and 12 other functionals Theor. Chem. Acc. 120, 215-241
    • (2008) Theor. Chem. Acc. , vol.120 , pp. 215-241
    • Zhao, Y.1    Truhlar, D.G.2
  • 52
    • 70549084886 scopus 로고    scopus 로고
    • Density functional theory for transition metals and transition metal chemistry
    • Cramer, C. J. and Truhlar, D. G. (2009) Density functional theory for transition metals and transition metal chemistry Phys. Chem. Chem. Phys. 11, 10757-10816
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 10757-10816
    • Cramer, C.J.1    Truhlar, D.G.2
  • 53
    • 18744387415 scopus 로고    scopus 로고
    • Chemical Theory and Computation Special Feature: Potential energy functions for atomic-level simulations of water and organic and biomolecular systems
    • Jorgensen, W. L. and Tirado-Rives, J. (2005) Chemical Theory and Computation Special Feature: Potential energy functions for atomic-level simulations of water and organic and biomolecular systems Proc. Natl. Acad. Sci. U.S.A. 102, 6665-6670
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6665-6670
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 54
    • 26744445949 scopus 로고
    • Dynamic force field models: Molecular dynamics simulations of human carbonic anhydrase II using a quantum mechanical/molecular mechanical coupled potential
    • Hartsough, D. S. and Merz, K. M. (1995) Dynamic force field models: Molecular dynamics simulations of human carbonic anhydrase II using a quantum mechanical/molecular mechanical coupled potential J. Phys. Chem. 99, 11266-11275
    • (1995) J. Phys. Chem. , vol.99 , pp. 11266-11275
    • Hartsough, D.S.1    Merz, K.M.2
  • 55
    • 34547511107 scopus 로고    scopus 로고
    • Implementation of the SCC-DFTB method for hybrid QM/MM simulations within the Amber molecular dynamics package
    • Seabra, G. D., Walker, R. C., Elstner, M., Case, D. A., and Roitberg, A. E. (2007) Implementation of the SCC-DFTB method for hybrid QM/MM simulations within the Amber molecular dynamics package J. Phys. Chem. A 111, 5655-5664
    • (2007) J. Phys. Chem. A , vol.111 , pp. 5655-5664
    • Seabra, G.D.1    Walker, R.C.2    Elstner, M.3    Case, D.A.4    Roitberg, A.E.5
  • 56
    • 79954547473 scopus 로고    scopus 로고
    • DFTB3: Extension of the self-consistent-charge density-functional tight-binding method (SCC-DFTB)
    • Gaus, M., Cui, Q. A., and Elstner, M. (2011) DFTB3: Extension of the self-consistent-charge density-functional tight-binding method (SCC-DFTB) J. Chem. Theory Comput. 7, 931-948
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 931-948
    • Gaus, M.1    Cui, Q.A.2    Elstner, M.3
  • 57
    • 82555168477 scopus 로고    scopus 로고
    • Insight into the cation-π interaction at the metal binding site of the copper metallochaperone CusF
    • Chakravorty, D. K., Wang, B., Ucisik, M. N., and Merz, K. M. (2011) Insight into the cation-π interaction at the metal binding site of the copper metallochaperone CusF J. Am. Chem. Soc. 133, 19330-19333
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19330-19333
    • Chakravorty, D.K.1    Wang, B.2    Ucisik, M.N.3    Merz, K.M.4
  • 58
    • 84862908683 scopus 로고    scopus 로고
    • Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS
    • Yang, Y., Wang, B., Ucisik, M. N., Cui, G., Fierke, C. A., and Merz, K. M. (2012) Insights into the mechanistic dichotomy of the protein farnesyltransferase peptide substrates CVIM and CVLS J. Am. Chem. Soc. 134, 820-823
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 820-823
    • Yang, Y.1    Wang, B.2    Ucisik, M.N.3    Cui, G.4    Fierke, C.A.5    Merz, K.M.6
  • 60
    • 36549091806 scopus 로고
    • A Complete Basis Set Model Chemistry. 1. The Total Energies of Closed-Shell Atoms and Hydrides of the 1st-Row Elements
    • Petersson, G. A., Bennett, A., Tensfeldt, T. G., Allaham, M. A., Shirley, W. A., and Mantzaris, J. (1988) A Complete Basis Set Model Chemistry. 1. The Total Energies of Closed-Shell Atoms and Hydrides of the 1st-Row Elements J. Chem. Phys. 89, 2193-2218
    • (1988) J. Chem. Phys. , vol.89 , pp. 2193-2218
    • Petersson, G.A.1    Bennett, A.2    Tensfeldt, T.G.3    Allaham, M.A.4    Shirley, W.A.5    Mantzaris, J.6
  • 61
    • 0038035472 scopus 로고
    • A Complete Basis Set Model Chemistry. 2. Open-Shell Systems and the Total Energies of the 1st-Row Atoms
    • Petersson, G. A. and Allaham, M. A. (1991) A Complete Basis Set Model Chemistry. 2. Open-Shell Systems and the Total Energies of the 1st-Row Atoms J. Chem. Phys. 94, 6081-6090
    • (1991) J. Chem. Phys. , vol.94 , pp. 6081-6090
    • Petersson, G.A.1    Allaham, M.A.2
  • 62
    • 0006073669 scopus 로고
    • Ab initio effective core potentials for molecular calculations: Potentials for main group elements Na to Bi
    • Wadt, W. R. and Hay, P. J. (1985) Ab initio effective core potentials for molecular calculations: Potentials for main group elements Na to Bi J. Chem. Phys. 82, 284-298
    • (1985) J. Chem. Phys. , vol.82 , pp. 284-298
    • Wadt, W.R.1    Hay, P.J.2
  • 63
    • 50249098941 scopus 로고    scopus 로고
    • Revised basis sets for the LANL effective core potentials
    • Roy, L. E., Hay, P. J., and Martin, R. L. (2008) Revised basis sets for the LANL effective core potentials J. Chem. Theory Comput. 4, 1029-1031
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 1029-1031
    • Roy, L.E.1    Hay, P.J.2    Martin, R.L.3
  • 64
    • 77956608400 scopus 로고    scopus 로고
    • Structural survey of zinc-containing proteins and development of the zinc AMBER force field (ZAFF)
    • Peters, M. B., Yang, Y., Wang, B., Fusti-Molnar, L., Weaver, M. N., and Merz, K. M. (2010) Structural survey of zinc-containing proteins and development of the zinc AMBER force field (ZAFF) J. Chem. Theory Comput. 6, 2935-2947
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 2935-2947
    • Peters, M.B.1    Yang, Y.2    Wang, B.3    Fusti-Molnar, L.4    Weaver, M.N.5    Merz, K.M.6
  • 66
    • 0033654297 scopus 로고    scopus 로고
    • Generalized Born models of macromolecular solvation effects
    • Bashford, D. and Case, D. A. (2000) Generalized Born models of macromolecular solvation effects Annu. Rev. Phys. Chem. 51, 129-152
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 67
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free-energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate calculation of hydration free-energies using macroscopic solvent models J. Phys. Chem. 98, 1978-1988
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 69
    • 20444466105 scopus 로고    scopus 로고
    • Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor
    • Ye, J., Kandegedara, A., Martin, P., and Rosen, B. P. (2005) Crystal structure of the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)- responsive repressor J. Bacteriol. 187, 4214-4221
    • (2005) J. Bacteriol. , vol.187 , pp. 4214-4221
    • Ye, J.1    Kandegedara, A.2    Martin, P.3    Rosen, B.P.4
  • 70
    • 0032536158 scopus 로고    scopus 로고
    • Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins
    • Cook, W. J., Kar, S. R., Taylor, K. B., and Hall, L. M. (1998) Crystal structure of the cyanobacterial metallothionein repressor SmtB: A model for metalloregulatory proteins J. Mol. Biol. 275, 337-346
    • (1998) J. Mol. Biol. , vol.275 , pp. 337-346
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 71
    • 84857861036 scopus 로고    scopus 로고
    • Metal site occupancy and allosteric switching in bacterial metal sensor proteins
    • Guerra, A. J. and Giedroc, D. P. (2011) Metal site occupancy and allosteric switching in bacterial metal sensor proteins Arch. Biochem. Biophys. 519, 210-222
    • (2011) Arch. Biochem. Biophys. , vol.519 , pp. 210-222
    • Guerra, A.J.1    Giedroc, D.P.2
  • 72
    • 0037031312 scopus 로고    scopus 로고
    • Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB
    • VanZile, M. L., Chen, X., and Giedroc, D. P. (2002) Structural characterization of distinct α3N and α5 metal sites in the cyanobacterial zinc sensor SmtB Biochemistry 41, 9765-9775
    • (2002) Biochemistry , vol.41 , pp. 9765-9775
    • Vanzile, M.L.1    Chen, X.2    Giedroc, D.P.3
  • 73
    • 33645466012 scopus 로고    scopus 로고
    • A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings
    • Pochapsky, T. C., Pochapsky, S. S., Ju, T., Hoefler, C., and Liang, J. (2006) A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings J. Biomol. NMR 34, 117-127
    • (2006) J. Biomol. NMR , vol.34 , pp. 117-127
    • Pochapsky, T.C.1    Pochapsky, S.S.2    Ju, T.3    Hoefler, C.4    Liang, J.5
  • 74
    • 39549101999 scopus 로고    scopus 로고
    • 15N double-quantum spectroscopy permits sequential resonance assignments near a paramagnetic center in acireductone dioxygenase
    • 15N double-quantum spectroscopy permits sequential resonance assignments near a paramagnetic center in acireductone dioxygenase J. Am. Chem. Soc. 130, 2156-2157
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2156-2157
    • Pochapsky, S.S.1    Sunshine, J.C.2    Pochapsky, T.C.3
  • 77
    • 10844293517 scopus 로고    scopus 로고
    • ATCUN-like metal-binding motifs in proteins: Identification and characterization by crystal structure and sequence analysis
    • Sankararamakrishnan, R., Verma, S., and Kumar, S. (2005) ATCUN-like metal-binding motifs in proteins: Identification and characterization by crystal structure and sequence analysis Proteins 58, 211-221
    • (2005) Proteins , vol.58 , pp. 211-221
    • Sankararamakrishnan, R.1    Verma, S.2    Kumar, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.