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Volumn 188, Issue 16, 2006, Pages 5993-6001

Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; ARGININE; BACTERIAL PROTEIN; HEAT SHOCK PROTEIN; MONOMER; PROTEIN RV2302; SOLVENT; UNCLASSIFIED DRUG;

EID: 33748665774     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00460-06     Document Type: Article
Times cited : (7)

References (45)
  • 1
    • 0036270739 scopus 로고    scopus 로고
    • Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
    • Betts, J. C., P. T. Lukey, L. C. Robb, R. A. McAdam, and K. Duncan. 2002. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol. Microbiol. 43:717-731.
    • (2002) Mol. Microbiol. , vol.43 , pp. 717-731
    • Betts, J.C.1    Lukey, P.T.2    Robb, L.C.3    McAdam, R.A.4    Duncan, K.5
  • 3
    • 0034633954 scopus 로고    scopus 로고
    • Spectroscopic studies of zinc(II)- and colbalt(II)-associated Escherichia coli formamidopyrimidine-DNA glycosylase: Extended X-ray absorption fine structure evidence for a metal-binding domain
    • Buchko, G. W., N. J. Hess, V. Bandaru, S. S. Wallace, and M. A. Kennedy. 2000. Spectroscopic studies of zinc(II)- and colbalt(II)-associated Escherichia coli formamidopyrimidine-DNA glycosylase: extended X-ray absorption fine structure evidence for a metal-binding domain. Biochemistry 40:12441-12449.
    • (2000) Biochemistry , vol.40 , pp. 12441-12449
    • Buchko, G.W.1    Hess, N.J.2    Bandaru, V.3    Wallace, S.S.4    Kennedy, M.A.5
  • 4
    • 12344315791 scopus 로고    scopus 로고
    • Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): A dynamic description of the DNA/protein interface
    • Buchko, G. W., K. McAteer, S. S. Wallace, and M. A. Kennedy. 2005. Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface. DNA Repair 4:327-339.
    • (2005) DNA Repair , vol.4 , pp. 327-339
    • Buchko, G.W.1    McAteer, K.2    Wallace, S.S.3    Kennedy, M.A.4
  • 5
    • 0015914783 scopus 로고
    • Conformation of twisted β-pleated sheets in proteins
    • Chothia, C. 1973. Conformation of twisted β-pleated sheets in proteins. J. Mol. Biol. 75:295-302.
    • (1973) J. Mol. Biol. , vol.75 , pp. 295-302
    • Chothia, C.1
  • 7
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., F. Delagio, and A. Bax. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13:289-301.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-301
    • Cornilescu, G.1    Delagio, F.2    Bax, A.3
  • 11
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., T. Pupko, I. Paz, R. E. Bell, D. Bechor-Shental, E. Martz, and N. Ben-Tal. 2003. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19:163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 13
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L., and C. Sander. 1998. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26:316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 14
    • 11344291497 scopus 로고
    • The ultra-violet circular dichroism of polypeptides
    • Holzwarth, G. M., and P. Doty. 1965. The ultra-violet circular dichroism of polypeptides. J. Am. Chem. Soc. 87:218-228.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 218-228
    • Holzwarth, G.M.1    Doty, P.2
  • 16
    • 44949267857 scopus 로고
    • Improved proton-detected heteronuclear correlations using gradient-enhanced Z and ZZ filters
    • John, B. K., D. Plant, and R. E. Hurd. 1993. Improved proton-detected heteronuclear correlations using gradient-enhanced Z and ZZ filters. J. Magn. Reson. B 101:113-117.
    • (1993) J. Magn. Reson. B , vol.101 , pp. 113-117
    • John, B.K.1    Plant, D.2    Hurd, R.E.3
  • 18
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlated spectroscopy with improved sensitivity
    • Kay, L. E., P. Keifer, and T. Saarinen. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlated spectroscopy with improved sensitivity. J. Amer. Chem. Soc. 114:10663-10665.
    • (1992) J. Amer. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., M. Billeter, and K. Wuthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14:51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Cryst. 24:946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0041315637 scopus 로고    scopus 로고
    • Clustering of large hydrophobes in the hydrophobic core of two-stranded α-helical coiled-coils controls protein folding and stability
    • Kwok, S. C., and R. S. Hodges. 2003. Clustering of large hydrophobes in the hydrophobic core of two-stranded α-helical coiled-coils controls protein folding and stability. J. Biol. Chem. 278:35248-35254.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35248-35254
    • Kwok, S.C.1    Hodges, R.S.2
  • 23
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., J. A. C. Rullmann, M. W. MacArthur, R. Kaptein, and J. M. Thornton. 1996. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8:477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 24
    • 0033064496 scopus 로고    scopus 로고
    • Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
    • Linge, J. P., and M. Nilges. 1999. Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation. J. Biomol. NMR 13:51-59.
    • (1999) J. Biomol. NMR , vol.13 , pp. 51-59
    • Linge, J.P.1    Nilges, M.2
  • 25
    • 0027568083 scopus 로고
    • A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments
    • Logan, T. M., E. T. Olejniczak, R. X. Xu, and S. W. Fesik. 1993. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J. Biomol. NMR 3:225-231.
    • (1993) J. Biomol. NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 26
    • 0001590904 scopus 로고
    • 13C isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins
    • 13C isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins. J. Magn. Res. B 101:206-209.
    • (1993) J. Magn. Res. B , vol.101 , pp. 206-209
    • Lyons, B.A.1    Montelione, G.T.2
  • 27
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease H1-correlations with structure and function in an active enzyme
    • Mandel, A. M., M. Akke, and A. G. Palmer III. 1995. Backbone dynamics of Escherichia coli ribonuclease H1-correlations with structure and function in an active enzyme. J. Mol. Biol. 246:144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 28
    • 0024065282 scopus 로고
    • Circular dichroism studies of distorted α-helices, twisted β-sheets and β-turns
    • Manning, C. M., M. Illangaseke, and R. W. Woody. 1988. Circular dichroism studies of distorted α-helices, twisted β-sheets and β-turns. Biophys. Chem. 31:77-86.
    • (1988) Biophys. Chem. , vol.31 , pp. 77-86
    • Manning, C.M.1    Illangaseke, M.2    Woody, R.W.3
  • 29
    • 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., B. A. Lyons, S. D. Emerson, and M. Tashiro. 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
  • 30
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-reso-nance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and L. E. Kay. 1994. Gradient-enhanced triple-reso-nance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103:203-216.
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 31
    • 0024435833 scopus 로고
    • Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling
    • Neri, D., T. Szyperski, G. Otting, H. Senn, and K. Wütrich. 1989. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling. Biochemistry 28:7510-7516.
    • (1989) Biochemistry , vol.28 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wütrich, K.5
  • 32
    • 11844292002 scopus 로고    scopus 로고
    • Inference of protein function from protein structure
    • Pal, D., and D. Eisenberg. 2005. Inference of protein function from protein structure. Structure 13:121-130.
    • (2005) Structure , vol.13 , pp. 121-130
    • Pal, D.1    Eisenberg, D.2
  • 35
    • 0019263093 scopus 로고
    • Reverse turns in peptides and proteins
    • Smith, J. A., and L. G. Pease. 1980. Reverse turns in peptides and proteins. CRC Crit. Rev. Biochem. 8:315-399.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 315-399
    • Smith, J.A.1    Pease, L.G.2
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0003481472 scopus 로고    scopus 로고
    • World Health Organization, Geneva, Switzerland
    • World Health Organization. 2005. Tuberculosis fact sheet no. 104. World Health Organization, Geneva, Switzerland.
    • (2005) Tuberculosis Fact Sheet No. 104
  • 45
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed-field gradient NMR techniques. J. Biomol. NMR 4:845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


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