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Volumn 403, Issue 3, 2010, Pages 468-479

The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage λ Tail Tube Protein

Author keywords

Bacteriophage lambda; GpV; Ig like domain; NMR structure; Phage tail

Indexed keywords

BACTERIAL PROTEIN; DOUBLE STRANDED DNA; IMMUNOGLOBULIN; VIRUS PROTEIN;

EID: 77957752176     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.044     Document Type: Article
Times cited : (40)

References (46)
  • 1
    • 33646191863 scopus 로고    scopus 로고
    • Ig-like domains on bacteriophages: a tale of promiscuity and deceit
    • Fraser J.S., Yu Z., Maxwell K.L., Davidson A.R. Ig-like domains on bacteriophages: a tale of promiscuity and deceit. J. Mol. Biol. 2006, 359:496-507.
    • (2006) J. Mol. Biol. , vol.359 , pp. 496-507
    • Fraser, J.S.1    Yu, Z.2    Maxwell, K.L.3    Davidson, A.R.4
  • 2
    • 0021351884 scopus 로고
    • Proteinase sensitivity of bacteriophage lambda tail proteins gpJ and pH in complexes with the lambda receptor
    • Roessner C.A., Ihler G.M. Proteinase sensitivity of bacteriophage lambda tail proteins gpJ and pH in complexes with the lambda receptor. J. Bacteriol. 1984, 157:165-170.
    • (1984) J. Bacteriol. , vol.157 , pp. 165-170
    • Roessner, C.A.1    Ihler, G.M.2
  • 3
    • 0030761567 scopus 로고    scopus 로고
    • A member of the immunoglobulin superfamily in bacteriophage T4
    • Bateman A., Eddy S.R., Mesyanzhinov V.V. A member of the immunoglobulin superfamily in bacteriophage T4. Virus Genes 1997, 14:163-165.
    • (1997) Virus Genes , vol.14 , pp. 163-165
    • Bateman, A.1    Eddy, S.R.2    Mesyanzhinov, V.V.3
  • 5
    • 33746931256 scopus 로고    scopus 로고
    • Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships
    • Effantin G., Boulanger P., Neumann E., Letellier L., Conway J.F. Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships. J. Mol. Biol. 2006, 361:993-1002.
    • (2006) J. Mol. Biol. , vol.361 , pp. 993-1002
    • Effantin, G.1    Boulanger, P.2    Neumann, E.3    Letellier, L.4    Conway, J.F.5
  • 6
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29
    • Morais M.C., Choi K.H., Koti J.S., Chipman P.R., Anderson D.L., Rossmann M.G. Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29. Mol. Cell 2005, 18:149-159.
    • (2005) Mol. Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 7
    • 1542317103 scopus 로고    scopus 로고
    • A -1 ribosomal frameshift in the transcript that encodes the major head protein of bacteriophage A2 mediates biosynthesis of a second essential component of the capsid
    • Garcia P., Rodriguez I., Suarez J.E. A -1 ribosomal frameshift in the transcript that encodes the major head protein of bacteriophage A2 mediates biosynthesis of a second essential component of the capsid. J. Bacteriol. 2004, 186:1714-1719.
    • (2004) J. Bacteriol. , vol.186 , pp. 1714-1719
    • Garcia, P.1    Rodriguez, I.2    Suarez, J.E.3
  • 8
    • 0024353628 scopus 로고
    • Nucleotide sequence and complementation studies of the gene 10 region of bacteriophage T3
    • Condreay J.P., Wright S.E., Molineux I.J. Nucleotide sequence and complementation studies of the gene 10 region of bacteriophage T3. J. Mol. Biol. 1989, 207:555-561.
    • (1989) J. Mol. Biol. , vol.207 , pp. 555-561
    • Condreay, J.P.1    Wright, S.E.2    Molineux, I.J.3
  • 9
    • 0019799116 scopus 로고
    • Structure and function of the major tail protein of bacteriophage lambda. Mutants having small major tail protein molecules in their virion
    • Katsura I. Structure and function of the major tail protein of bacteriophage lambda. Mutants having small major tail protein molecules in their virion. J. Mol. Biol. 1981, 146:493-512.
    • (1981) J. Mol. Biol. , vol.146 , pp. 493-512
    • Katsura, I.1
  • 10
    • 61849155151 scopus 로고    scopus 로고
    • The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
    • Pell L.G., Kanelis V., Donaldson L.W., Howell P.L., Davidson A.R. The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc. Natl Acad. Sci. USA 2009, 106:4160-4165.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4160-4165
    • Pell, L.G.1    Kanelis, V.2    Donaldson, L.W.3    Howell, P.L.4    Davidson, A.R.5
  • 11
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 1999, 13:289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 12
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 1996, 8:477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 13
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P., Holm L., Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 1994, 242:309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 14
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 16
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterization of chemical exchange by NMR spectroscopy
    • Loria J.P., Rance M., Palmer A.G.I.I.I. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterization of chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 1999, 121:2331-2332.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer, A.G.I.I.I.3
  • 17
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 1995, 20:478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 18
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y., Godzik A. Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 2003, 19(Suppl. 2):ii246-ii255.
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL. 2
    • Ye, Y.1    Godzik, A.2
  • 19
    • 0032780181 scopus 로고    scopus 로고
    • Situs: a package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 1999, 125:185-195.
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 20
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with X-ray crystallographic structures
    • Rossmann M.G., Bernal R., Pletnev S.V. Combining electron microscopic with X-ray crystallographic structures. J. Struct. Biol. 2001, 136:190-200.
    • (2001) J. Struct. Biol. , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 21
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family: sequence analysis and 3D structure comparisons
    • Halaby D.M., Poupon A., Mornon J. The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Protein Eng. 1999, 12:563-571.
    • (1999) Protein Eng. , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.3
  • 22
    • 0031979387 scopus 로고    scopus 로고
    • The immunoglobulin superfamily: an insight on its tissular, species, and functional diversity
    • Halaby D.M., Mornon J.P. The immunoglobulin superfamily: an insight on its tissular, species, and functional diversity. J. Mol. Evol. 1998, 46:389-400.
    • (1998) J. Mol. Evol. , vol.46 , pp. 389-400
    • Halaby, D.M.1    Mornon, J.P.2
  • 23
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 1994, 238:528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 24
    • 34548671924 scopus 로고    scopus 로고
    • Immunoglobulin-like domains on bacteriophage: weapons of modest damage?
    • Fraser J.S., Maxwell K.L., Davidson A.R. Immunoglobulin-like domains on bacteriophage: weapons of modest damage?. Curr. Opin. Microbiol. 2007, 10:382-387.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 382-387
    • Fraser, J.S.1    Maxwell, K.L.2    Davidson, A.R.3
  • 25
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann E., Ochs B., Abel K.J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 1988, 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 26
    • 4644282820 scopus 로고    scopus 로고
    • Complex spatial distribution and dynamics of an abundant Escherichia coli outer membrane protein, LamB
    • Gibbs K.A., Isaac D.D., Xu J., Hendrix R.W., Silhavy T.J., Theriot J.A. Complex spatial distribution and dynamics of an abundant Escherichia coli outer membrane protein, LamB. Mol. Microbiol. 2004, 53:1771-1783.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1771-1783
    • Gibbs, K.A.1    Isaac, D.D.2    Xu, J.3    Hendrix, R.W.4    Silhavy, T.J.5    Theriot, J.A.6
  • 28
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 29
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 2004, 278:313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 30
    • 0036189601 scopus 로고    scopus 로고
    • Multidimensional NMR methods for protein structure determination
    • Kanelis V., Forman-Kay J.D., Kay L.E. Multidimensional NMR methods for protein structure determination. IUBMB Life 2001, 52:291-302.
    • (2001) IUBMB Life , vol.52 , pp. 291-302
    • Kanelis, V.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 31
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay L.E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog. Biophys. Mol. Biol. 1995, 63:277-299.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 32
    • 12044258763 scopus 로고
    • Two-dimensional NMR experiments for correlating carbon-13beta and proton delta/epsilon chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings
    • Yamazaki T., Forman-Kay J.D., Kay L.E. Two-dimensional NMR experiments for correlating carbon-13beta and proton delta/epsilon chemical shifts of aromatic residues in 13C-labeled proteins via scalar couplings. J. Am. Chem. Soc. 1993, 115:11054-11055.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11054-11055
    • Yamazaki, T.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 33
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 2004, 278:353-378.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996, 14:51-55. 29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 35
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer A.G., Kroenke C.D., Loria J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 2001, 339:204-238.
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 36
    • 0034981892 scopus 로고    scopus 로고
    • MUNIN: a new approach to multi-dimensional NMR spectra interpretation
    • Orekhov V.Y., Ibraghimov I.V., Billeter M. MUNIN: a new approach to multi-dimensional NMR spectra interpretation. J. Biomol. NMR 2001, 20:49-60.
    • (2001) J. Biomol. NMR , vol.20 , pp. 49-60
    • Orekhov, V.Y.1    Ibraghimov, I.V.2    Billeter, M.3
  • 37
    • 0035211558 scopus 로고    scopus 로고
    • MUNIN: application of three-way decomposition to the analysis of heteronuclear NMR relaxation data
    • Korzhnev D.M., Ibraghimov I.V., Billeter M., Orekhov V.Y. MUNIN: application of three-way decomposition to the analysis of heteronuclear NMR relaxation data. J. Biomol. NMR 2001, 21:263-268.
    • (2001) J. Biomol. NMR , vol.21 , pp. 263-268
    • Korzhnev, D.M.1    Ibraghimov, I.V.2    Billeter, M.3    Orekhov, V.Y.4
  • 39
    • 23144457893 scopus 로고    scopus 로고
    • Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters
    • Ishima R., Torchia D.A. Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters. J. Biomol. NMR 2005, 32:41-54.
    • (2005) J. Biomol. NMR , vol.32 , pp. 41-54
    • Ishima, R.1    Torchia, D.A.2
  • 40
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell H.M. Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 1958, 28.
    • (1958) J. Chem. Phys. , pp. 28
    • McConnell, H.M.1
  • 41
    • 27644432794 scopus 로고    scopus 로고
    • Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant
    • Korzhnev D.M., Neudecker P., Mittermaier A., Orekhov V.Y., Kay L.E. Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant. J. Am. Chem. Soc. 2005, 127:15602-15611.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15602-15611
    • Korzhnev, D.M.1    Neudecker, P.2    Mittermaier, A.3    Orekhov, V.Y.4    Kay, L.E.5
  • 43
    • 33645793984 scopus 로고    scopus 로고
    • Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain
    • Neudecker P., Korzhnev D.M., Kay L.E. Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain. J. Biomol. NMR 2006, 34:129-135.
    • (2006) J. Biomol. NMR , vol.34 , pp. 129-135
    • Neudecker, P.1    Korzhnev, D.M.2    Kay, L.E.3
  • 46
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K., Misawa K., Kuma K., Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 2002, 30:3059-3066.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4


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