메뉴 건너뛰기




Volumn 37, Issue 6, 2008, Pages 1077-1082

The hand of the filamentous bacteriophage helix

Author keywords

Helix; Fibre diffraction; Solid state NMR

Indexed keywords

HELIX LOOP HELIX PROTEIN; PROTEIN SUBUNIT;

EID: 45849151693     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0327-7     Document Type: Article
Times cited : (4)

References (30)
  • 2
    • 0020805510 scopus 로고
    • Maximum-entropy calculation of the electron density at 4 Å resolution of Pf1 filamentous bacteriophage
    • Bryan RK, Bansal M, Folkhard W, Nave C, Marvin DA (1983) Maximum-entropy calculation of the electron density at 4 Å resolution of Pf1 filamentous bacteriophage. Proc Natl Acad Sci USA 80:4728-4731
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4728-4731
    • Bryan, R.K.1    Bansal, M.2    Folkhard, W.3    Nave, C.4    Marvin, D.A.5
  • 3
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick FHC (1953) The packing of α-helices: simple coiled-coils. Acta Crystallogr 6:689-697
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 5
    • 33847628307 scopus 로고    scopus 로고
    • Filamentous phage studied by magic-angle spinning NMR: Resonance assignment and secondary structure of the coat protein in Pf1
    • Goldbourt A, Gross BJ, Day LA, McDermott AE (2007) Filamentous phage studied by magic-angle spinning NMR: resonance assignment and secondary structure of the coat protein in Pf1. J Am Chem Soc 129:2338-2344
    • (2007) J Am Chem Soc , vol.129 , pp. 2338-2344
    • Goldbourt, A.1    Gross, B.J.2    Day, L.A.3    McDermott, A.E.4
  • 6
    • 0000568172 scopus 로고
    • Pf1 filamentous bacteriophage: Refinement of a molecular model by simulated annealing using 3.3Å resolution X-ray fibre diffraction data
    • Gonzalez A, Nave C, Marvin DA (1995) Pf1 filamentous bacteriophage: Refinement of a molecular model by simulated annealing using 3.3Å resolution X-ray fibre diffraction data. Acta Crystallogr Sect D 51:792-804
    • (1995) Acta Crystallogr Sect D , vol.51 , pp. 792-804
    • Gonzalez, A.1    Nave, C.2    Marvin, D.A.3
  • 7
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the Swiss-PDB viewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) Swiss-model and the Swiss-PDB viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 8
    • 0034130999 scopus 로고    scopus 로고
    • Filamentous bacteriophage for aligning RNA, DNA, and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions
    • Hansen MR, Hanson P, Pardi A (2000) Filamentous bacteriophage for aligning RNA, DNA, and proteins for measurement of nuclear magnetic resonance dipolar coupling interactions. Methods Enzymol. 317:220-240
    • (2000) Methods Enzymol. , vol.317 , pp. 220-240
    • Hansen, M.R.1    Hanson, P.2    Pardi, A.3
  • 10
    • 0030831667 scopus 로고    scopus 로고
    • α coordinates alone
    • α coordinates alone. J Mol Biol 273:371-376
    • (1997) J Mol Biol , vol.273 , pp. 371-376
    • Kleywegt, G.J.1
  • 11
    • 0019201172 scopus 로고
    • Filamentous bacteriophage Pf1 structure determined at 7 Å resolution by refinement of models for the α-helical subunit
    • Makowski L, Caspar DLD, Marvin DA (1980) Filamentous bacteriophage Pf1 structure determined at 7 Å resolution by refinement of models for the α-helical subunit. J Mol Biol 140:149-181
    • (1980) J Mol Biol , vol.140 , pp. 149-181
    • Makowski, L.1    Caspar, D.L.D.2    Marvin, D.A.3
  • 12
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi FM, Opella SJ (2000) A solid-state NMR index of helical membrane protein structure and topology. J Magn Reson 144:150-155
    • (2000) J Magn Reson , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 13
    • 0036361158 scopus 로고    scopus 로고
    • Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins
    • Marassi FM, Opella SJ (2002) Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins. J Biomol NMR 23:239-242
    • (2002) J Biomol NMR , vol.23 , pp. 239-242
    • Marassi, F.M.1    Opella, S.J.2
  • 14
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi FM, Opella SJ (2003) Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci 12:403-411
    • (2003) Protein Sci , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 15
    • 0017319019 scopus 로고
    • Structure and assembly of filamentous bacterial viruses
    • Marvin DA, Wachtel EJ (1976) Structure and assembly of filamentous bacterial viruses. Philos Trans R Soc Lond Ser B 276:81-98
    • (1976) Philos Trans R Soc Lond Ser B , vol.276 , pp. 81-98
    • Marvin, D.A.1    Wachtel, E.J.2
  • 17
    • 0023123048 scopus 로고
    • Pf1 Inovirus: Electron density distribution calculated by a maximum entropy algorithm from native fibre diffraction data to 3 Å resolution and single isomorphous replacement data to 5 Å resolution
    • Marvin DA, Bryan RK, Nave C (1987) Pf1 Inovirus: electron density distribution calculated by a maximum entropy algorithm from native fibre diffraction data to 3 Å resolution and single isomorphous replacement data to 5 Å resolution. J Mol Biol 193:315-343
    • (1987) J Mol Biol , vol.193 , pp. 315-343
    • Marvin, D.A.1    Bryan, R.K.2    Nave, C.3
  • 18
    • 0028058295 scopus 로고
    • Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe
    • Marvin DA, Hale RD, Nave C, Helmer-Citterich M (1994) Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe. J Mol Biol 235:260-286
    • (1994) J Mol Biol , vol.235 , pp. 260-286
    • Marvin, D.A.1    Hale, R.D.2    Nave, C.3    Helmer-Citterich, M.4
  • 19
    • 28844441971 scopus 로고    scopus 로고
    • Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane
    • Marvin DA, Welsh LC, Symmons MF, Scott WRP, Straus SK (2006) Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane. J Mol Biol 355:294-309
    • (2006) J Mol Biol , vol.355 , pp. 294-309
    • Marvin, D.A.1    Welsh, L.C.2    Symmons, M.F.3    Scott, W.R.P.4    Straus, S.K.5
  • 20
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • Melo F, Feytmans E (1998) Assessing protein structures with a non-local atomic interaction energy. J Mol Biol 277:1141-1152
    • (1998) J Mol Biol , vol.277 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 21
    • 41049097811 scopus 로고    scopus 로고
    • Filamentous phage
    • 2nd edn Oxford University Press USA
    • Russel M, Model P (2006) Filamentous phage. In: Calendar R (ed) The bacteriophages, 2nd edn. Oxford University Press, USA, pp 146-160
    • (2006) The Bacteriophages , pp. 146-160
    • Russel, M.1    Model, P.2    Calendar, R.3
  • 24
    • 4344702276 scopus 로고    scopus 로고
    • Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy
    • Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ (2004) Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy. J Mol Biol 341:869-879
    • (2004) J Mol Biol , vol.341 , pp. 869-879
    • Thiriot, D.S.1    Nevzorov, A.A.2    Zagyanskiy, L.3    Wu, C.H.4    Opella, S.J.5
  • 25
    • 33745639488 scopus 로고    scopus 로고
    • Chiral nematic phase of suspensions of rodlike viruses: Left-handed phase helicity from a right-handed molecular helix
    • Tombolato F, Ferrarini A, Grelet E (2006) Chiral nematic phase of suspensions of rodlike viruses: left-handed phase helicity from a right-handed molecular helix. Phys Rev Lett 96:258302(4)
    • (2006) Phys Rev Lett , vol.96 , pp. 2583024
    • Tombolato, F.1    Ferrarini, A.2    Grelet, E.3
  • 26
    • 0027589340 scopus 로고
    • Molecular dynamics in refinement against fiber diffraction data
    • Wang H, Stubbs G (1993) Molecular dynamics in refinement against fiber diffraction data. Acta Crystallog Sect A 49:504-513
    • (1993) Acta Crystallog Sect a , vol.49 , pp. 504-513
    • Wang, H.1    Stubbs, G.2
  • 29
    • 0034142068 scopus 로고    scopus 로고
    • The molecular structure and structural transition of the α-helical capsid in filamentous bacteriophage Pf1
    • Welsh LC, Symmons MF, Marvin DA (2000) The molecular structure and structural transition of the α-helical capsid in filamentous bacteriophage Pf1. Acta Crystallogr Sect D 56:137-150
    • (2000) Acta Crystallogr Sect D , vol.56 , pp. 137-150
    • Welsh, L.C.1    Symmons, M.F.2    Marvin, D.A.3
  • 30
    • 0038652081 scopus 로고    scopus 로고
    • Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
    • Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ (2003) Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy. Proc Natl Acad Sci USA 100:6458-6463
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6458-6463
    • Zeri, A.C.1    Mesleh, M.F.2    Nevzorov, A.A.3    Opella, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.