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Volumn 17, Issue 6, 2009, Pages 800-808

The Structure of Gene Product 6 of Bacteriophage T4, the Hinge-Pin of the Baseplate

Author keywords

PROTEINS

Indexed keywords

GENE PRODUCT; GENE PRODUCT 6; UNCLASSIFIED DRUG;

EID: 66749084492     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.04.005     Document Type: Article
Times cited : (27)

References (33)
  • 1
    • 33847697902 scopus 로고    scopus 로고
    • Classification of bacteriophages
    • Calendar R. (Ed), Oxford University Press, New York, NY
    • Ackermann H.-W. Classification of bacteriophages. In: Calendar R. (Ed). The Bacteriophages (2006), Oxford University Press, New York, NY 8-16
    • (2006) The Bacteriophages , pp. 8-16
    • Ackermann, H.-W.1
  • 4
    • 84868093436 scopus 로고
    • A new least-squares refinement technique based on the fast Fourier transform algorithm
    • Agarwal R.C. A new least-squares refinement technique based on the fast Fourier transform algorithm. Acta Crystallogr. A 34 (1978) 791-809
    • (1978) Acta Crystallogr. A , vol.34 , pp. 791-809
    • Agarwal, R.C.1
  • 5
    • 0019764483 scopus 로고
    • Contraction and dissociation of the bacteriophage T4 tail sheath induced by heat and urea
    • Arisaka F., Engel J., and Horst K. Contraction and dissociation of the bacteriophage T4 tail sheath induced by heat and urea. Prog. Clin. Biol. Res. 64 (1981) 365-379
    • (1981) Prog. Clin. Biol. Res. , vol.64 , pp. 365-379
    • Arisaka, F.1    Engel, J.2    Horst, K.3
  • 6
    • 0002583957 scopus 로고
    • 'dm': an automated procedure for phase improvement by density modification
    • Cowtan K.D. 'dm': an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31 (1994) 34-38
    • (1994) Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.D.1
  • 7
    • 0017757241 scopus 로고
    • Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4
    • Crowther R.A., Lenk E.V., Kikuchi Y., and King J. Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. J. Mol. Biol. 116 (1977) 489-523
    • (1977) J. Mol. Biol. , vol.116 , pp. 489-523
    • Crowther, R.A.1    Lenk, E.V.2    Kikuchi, Y.3    King, J.4
  • 8
    • 66749170431 scopus 로고    scopus 로고
    • DeLano Scientific LLC, Palo Alto, CA
    • DeLano, W.L. (2008). The PyMOL molecular graphics system. DeLano Scientific LLC, Palo Alto, CA. http://www.pymol.org.
    • (2008)
    • DeLano, W.L.1
  • 10
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., and Sander C. Mapping the protein universe. Science 273 (1996) 595-602
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 11
    • 0016621820 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro
    • Kikuchi Y., and King J. Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro. J. Mol. Biol. 99 (1975) 645-672
    • (1975) J. Mol. Biol. , vol.99 , pp. 645-672
    • Kikuchi, Y.1    King, J.2
  • 12
    • 0016587670 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate
    • Kikuchi Y., and King J. Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate. J. Mol. Biol. 99 (1975) 673-694
    • (1975) J. Mol. Biol. , vol.99 , pp. 673-694
    • Kikuchi, Y.1    King, J.2
  • 13
    • 0016599239 scopus 로고
    • Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway
    • Kikuchi Y., and King J. Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway. J. Mol. Biol. 99 (1975) 695-716
    • (1975) J. Mol. Biol. , vol.99 , pp. 695-716
    • Kikuchi, Y.1    King, J.2
  • 19
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V., and Rossmann M.G. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 118 (2004) 419-429
    • (2004) Cell , vol.118 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 20
    • 0015867079 scopus 로고
    • Sheath of bacteriophage T4. III. Contraction mechanism deduced from partially contracted sheaths
    • Moody M.F. Sheath of bacteriophage T4. III. Contraction mechanism deduced from partially contracted sheaths. J. Mol. Biol. 80 (1973) 613-635
    • (1973) J. Mol. Biol. , vol.80 , pp. 613-635
    • Moody, M.F.1
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan V., Finch J.T., Graziano V., Lee P.L., and Sweet R.M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362 (1993) 219-223
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 24
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1371-1382
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1371-1382
    • Read, R.J.1
  • 26
    • 0036901176 scopus 로고    scopus 로고
    • Statistical density modification with non-crystallographic symmetry
    • Terwilliger T.C. Statistical density modification with non-crystallographic symmetry. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 2082-2086
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 2082-2086
    • Terwilliger, T.C.1
  • 27
    • 0014694376 scopus 로고
    • Disassembly of T-even bacteriophage into structural parts and subunits
    • To C.M., Kellenberger E., and Eisenstark A. Disassembly of T-even bacteriophage into structural parts and subunits. J. Mol. Biol. 46 (1969) 493-511
    • (1969) J. Mol. Biol. , vol.46 , pp. 493-511
    • To, C.M.1    Kellenberger, E.2    Eisenstark, A.3
  • 28
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Usón I., and Sheldrick G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9 (1999) 643-648
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 643-648
    • Usón, I.1    Sheldrick, G.M.2
  • 29
    • 0024360333 scopus 로고
    • Analysis of near-neighbor contacts in bacteriophage T4 wedges and hubless baseplates by using a cleavable chemical cross-linker
    • Watts N.R.M., and Coombs D.H. Analysis of near-neighbor contacts in bacteriophage T4 wedges and hubless baseplates by using a cleavable chemical cross-linker. J. Virol. 63 (1989) 2427-2436
    • (1989) J. Virol. , vol.63 , pp. 2427-2436
    • Watts, N.R.M.1    Coombs, D.H.2
  • 30
    • 0025139852 scopus 로고
    • Structure of the bacteriophage T4 baseplate as determined by chemical cross-linking
    • Watts N.R.M., and Coombs D.H. Structure of the bacteriophage T4 baseplate as determined by chemical cross-linking. J. Virol. 64 (1990) 143-154
    • (1990) J. Virol. , vol.64 , pp. 143-154
    • Watts, N.R.M.1    Coombs, D.H.2
  • 32
    • 0032780181 scopus 로고    scopus 로고
    • Situs: a package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., and McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125 (1999) 185-189
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-189
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 33
    • 0015588598 scopus 로고
    • Organization and function of bacteriophage T4 tail: I. Isolation of heat-sensitive T4 tail mutants
    • Yamamoto M., and Uchida H. Organization and function of bacteriophage T4 tail: I. Isolation of heat-sensitive T4 tail mutants. Virology 52 (1973) 234-245
    • (1973) Virology , vol.52 , pp. 234-245
    • Yamamoto, M.1    Uchida, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.