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Volumn 378, Issue 3-4, 1997, Pages 337-344

Interaction of Salmonella Phage P22 with Its O-Antigen Receptor Studied by X-Ray Crystallography

Author keywords

Endoglycosidase; Phage mutants; Protein folding; Receptor binding; Virus protein; helix

Indexed keywords

BACTERIOPHAGE RECEPTOR; GALACTOSE; O ANTIGEN; RHAMNOSE;

EID: 0030918248     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.3-4.337     Document Type: Article
Times cited : (29)

References (51)
  • 2
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U., Wu, S., Flaherty, K. M., and McKay, D. B. (1993). Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 72, 3357-3364.
    • (1993) EMBO J. , vol.72 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 3
    • 0029816431 scopus 로고    scopus 로고
    • Interactions of phage P22 tails with their cellular receptor. Salmonella o-antigen polysaccharide
    • Baxa, U., Steinbacher, S., Miller, S., Weintraub, A., Huber, R., and Seckler, R. (1996). Interactions of phage P22 tails with their cellular receptor. Salmonella o-antigen polysaccharide. Biophys. J. 77, 2040-2048.
    • (1996) Biophys. J. , vol.77 , pp. 2040-2048
    • Baxa, U.1    Steinbacher, S.2    Miller, S.3    Weintraub, A.4    Huber, R.5    Seckler, R.6
  • 4
    • 0029031409 scopus 로고
    • Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context
    • Beißinger, M., Lee, S. C., Steinbacher, S., Reinemer, P., Huber, R., Yu, M.-H., and Seckler, R. (1995). Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context. J. Mol. Biol. 249, 185-194.
    • (1995) J. Mol. Biol. , vol.249 , pp. 185-194
    • Beißinger, M.1    Lee, S.C.2    Steinbacher, S.3    Reinemer, P.4    Huber, R.5    Yu, M.-H.6    Seckler, R.7
  • 5
    • 0018842562 scopus 로고
    • Structure and function of the bacteriophage P22 tail protein
    • Berget, R.B., and Poteete, A. R. (1980). Structure and function of the bacteriophage P22 tail protein. J. Virol. 34, 234-243.
    • (1980) J. Virol. , vol.34 , pp. 234-243
    • Berget, R.B.1    Poteete, A.R.2
  • 6
    • 0027509618 scopus 로고
    • Interaction of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro
    • Brunschier, R., Danner, M., and Seckler, R. (1993). Interaction of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J. Biol. Chem. 268, 2767-2772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2767-2772
    • Brunschier, R.1    Danner, M.2    Seckler, R.3
  • 7
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa, N., Steipe, B., Demange, P., Eckerskorn, C., Kellermann, J., and Huber, R. (1995). High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur. J. Biochem. 230, 788-796.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 8
    • 0025867101 scopus 로고
    • Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase
    • Chen, B.-L., and King, J. (1991). Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase. Biochemistry 30, 6260-6269.
    • (1991) Biochemistry , vol.30 , pp. 6260-6269
    • Chen, B.-L.1    King, J.2
  • 9
    • 0027370268 scopus 로고
    • Mechanism of phage P22 tailspike protein folding mutations
    • Danner, M., and Seckler, R. (1993). Mechanism of phage P22 tailspike protein folding mutations. Protein Science 2, 1869-1881.
    • (1993) Protein Science , vol.2 , pp. 1869-1881
    • Danner, M.1    Seckler, R.2
  • 10
    • 0027165264 scopus 로고
    • Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain
    • Danner, M., Fuchs, A., Miller, S., and Seckler, R. (1993). Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain. Eur. J. Biochem. 275, 653-661.
    • (1993) Eur. J. Biochem. , vol.275 , pp. 653-661
    • Danner, M.1    Fuchs, A.2    Miller, S.3    Seckler, R.4
  • 11
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G., and Henrissat, B. (1995). Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 12
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, R., Charles. I. G., Fairweather, N. F., and Isaacs, N. W. (1996). Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 387, 90-92.
    • (1996) Nature , vol.387 , pp. 90-92
    • Emsley, R.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 13
    • 0017341368 scopus 로고
    • Adsoption of phage P22 to Salmonella typhimurium
    • Eriksson, U., and Lindberg, A. A. (1977). Adsoption of phage P22 to Salmonella typhimurium. J. Gen. Virol. 34, 207-221.
    • (1977) J. Gen. Virol. , vol.34 , pp. 207-221
    • Eriksson, U.1    Lindberg, A.A.2
  • 14
    • 0018365547 scopus 로고
    • Salmonella phage glycanases: substrate specificity of the phage P22 endorhamnosidase
    • Eriksson, U., Svenson, S. B., Lönngren, J., and Lindberg, A. A. (1979). Salmonella phage glycanases: substrate specificity of the phage P22 endo-rhamnosidase. J. Gen. Virol. 43, 503-511.
    • (1979) J. Gen. Virol. , vol.43 , pp. 503-511
    • Eriksson, U.1    Svenson, S.B.2    Lönngren, J.3    Lindberg, A.A.4
  • 15
    • 0025821345 scopus 로고
    • In vitro folding pathway of the P22 tailspike protein
    • Fuchs, A., Seiderer, C., and Seckler, R. (1991). In vitro folding pathway of the P22 tailspike protein. Biochemistry 30, 6598-6604.
    • (1991) Biochemistry , vol.30 , pp. 6598-6604
    • Fuchs, A.1    Seiderer, C.2    Seckler, R.3
  • 16
    • 0018846882 scopus 로고
    • Heterogeneity of antigen-side-chain length in lipopolysaccharide from Escherichia coli 0111, and Salmonella typhimurium LT2
    • Goldman, R. C., and Leive, L. (1980). Heterogeneity of antigen-side-chain length in lipopolysaccharide from Escherichia coli 0111 and Salmonella typhimurium LT2. Eur J. Biochem. 707, 145-153.
    • (1980) Eur J. Biochem. , vol.707 , pp. 145-153
    • Goldman, R.C.1    Leive, L.2
  • 17
    • 0019474427 scopus 로고
    • Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein II. Active mutant protein matured at 30
    • Goldenberg, D. P., and King, J. (1981). Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein II. Active mutant protein matured at 30. J. Mol. Biol. 145, 633-651.
    • (1981) J. Mol. Biol. , vol.145 , pp. 633-651
    • Goldenberg, D.P.1    King, J.2
  • 18
    • 1542563859 scopus 로고
    • Trimeric intermediates in the in vivo folding and assembly of the tail spike endorhamnosidase of bacteriophage P22
    • Goldenberg, D., and King, J. (1982). Trimeric intermediates in the in vivo folding and assembly of the tail spike endorhamnosidase of bacteriophage P22. Proc. Natl. Acad. Sci. USA. 79, 3403-3407.
    • (1982) Proc. Natl. Acad. Sci. USA. , vol.79 , pp. 3403-3407
    • Goldenberg, D.1    King, J.2
  • 19
    • 0023883586 scopus 로고
    • Formation of aggregates from athermolabile in vivo folding intermediate in P22 tailspike maturation
    • Haase-Pettingell, C., and King, J. (1988). Formation of aggregates from athermolabile in vivo folding intermediate in P22 tailspike maturation. J. Biol. Chem. 263, 4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.1    King, J.2
  • 20
    • 0001926296 scopus 로고    scopus 로고
    • Virus structure
    • 3. ed., N. B. Fields, D. M. Knipe, P. M. Howley et al eds., (Philadelphia, USA: Raven Publishers)
    • Harrison, S. C., Skehel, J. J., and Wiley, D. C. (1996). Virus structure. In: Fields Virology. 3. ed., N. B. Fields, D. M. Knipe, P. M. Howley et al., eds., (Philadelphia, USA: Raven Publishers), pp. 59-99.
    • (1996) Fields Virology , pp. 59-99
    • Harrison, S.C.1    Skehel, J.J.2    Wiley, D.C.3
  • 21
    • 0344036042 scopus 로고
    • The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase
    • Herrler, G., Rott, R., Klenk, H.-D., Müller, H.-R., Shukia, A. K., and Schauer, R. (1985). The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J. 1503-1506.
    • (1985) EMBO J. , pp. 1503-1506
    • Herrler, G.1    Rott, R.2    Klenk, H.-D.3    Müller, H.-R.4    Shukia, A.K.5    Schauer, R.6
  • 22
    • 0000278197 scopus 로고
    • In vitro morphogenesis of phage P22 from heads and base-plate parts
    • Israel, J. V., Anderson, T. F., and Levine, M. (1967). In vitro morphogenesis of phage P22 from heads and base-plate parts. Proc. Natl. Acad. Sci. USA 57, 284-291.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 284-291
    • Israel, J.V.1    Anderson, T.F.2    Levine, M.3
  • 23
    • 0017174830 scopus 로고
    • Enzymatic and molecular properties of base-plate parts of bacteriophage P22
    • Iwashita, S., and Kanegasaki, S. (1976). Enzymatic and molecular properties of base-plate parts of bacteriophage P22. Eur. J. Biochem. 65, 87-94.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 87-94
    • Iwashita, S.1    Kanegasaki, S.2
  • 24
    • 0030020116 scopus 로고    scopus 로고
    • A new efficient synthesis of acetytelluro-and acetylse-lenomethionine and their use in the biosynthesis of heavy-atom protein analogs
    • Karnbrock. W., Weyher, E. Budisa, N., Huber, R., and Moroder, L. (1996). A new efficient synthesis of acetytelluro-and acetylse-lenomethionine and their use in the biosynthesis of heavy-atom protein analogs. J. Am. Chem. Soc. 778, 913-914.
    • (1996) J. Am. Chem. Soc. , vol.778 , pp. 913-914
    • Karnbrock, W.1    Weyher, E.2    Budisa, N.3    Huber, R.4    Moroder, L.5
  • 25
    • 0011168280 scopus 로고
    • A typhoid variant and a new serological variation in the Salmonella group
    • Kauffmann. F. (1941). A typhoid variant and a new serological variation in the Salmonella group. J. Bacteriol. 47, 127-140.
    • (1941) J. Bacteriol. , vol.47 , pp. 127-140
    • Kauffmann, F.1
  • 26
    • 0030063114 scopus 로고    scopus 로고
    • Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates
    • King, J., Haase-Pettingell, C., Robinson. A. S. Speed., M., and Mitraki, A. (1996). Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates. FASEB J. 70, 57-66.
    • (1996) FASEB J. , vol.70 , pp. 57-66
    • King, J.1    Haase-Pettingell, C.2    Robinson, A.S.3    Speed, M.4    Mitraki, A.5
  • 27
    • 0029874435 scopus 로고    scopus 로고
    • A left-handed ß-helix revealed by the crystal structure of a carbonic anhydrase from the archeon Methanosarcina thermophile
    • Kisker, C., Schindelin, H., Alber, B. E., Ferry, J. G., and Rees, D. C. (1996). A left-handed ß-helix revealed by the crystal structure of a carbonic anhydrase from the archeon Methanosarcina thermophile. EMBO J. 75, 2323-2330.
    • (1996) EMBO J. , vol.75 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 29
    • 0000651639 scopus 로고
    • Bacteriophage surface carbohydrates and bacteriophage adsorption
    • I. Sutherland, ed. (New York: Academic Press)
    • Lindberg, A. A. (1977). Bacteriophage surface carbohydrates and bacteriophage adsorption. In: Surface Carbohydrates of the Procaryotic Cell, I. Sutherland, ed. (New York: Academic Press) pp. 289-356.
    • (1977) Surface Carbohydrates of the Procaryotic Cell , pp. 289-356
    • Lindberg, A.A.1
  • 31
    • 0025333088 scopus 로고
    • Intragenic suppression of a capsid assembly-defective P22 tailspike mutation
    • Maurides, RA., Schwarz, J. J., and Berget, P. B. (1990). Intragenic suppression of a capsid assembly-defective P22 tailspike mutation. Genetics 725, 673-681.
    • (1990) Genetics , vol.725 , pp. 673-681
    • Maurides, R.A.1    Schwarz, J.J.2    Berget, P.B.3
  • 33
    • 0003611470 scopus 로고
    • Deletions-und Punktmutanten des P22 Tail-spike-Proteins
    • Ph. D. Thesis, Universität Regensburg
    • Miller, S. (1995). Deletions-und Punktmutanten des P22 Tail-spike-Proteins. Ph. D. Thesis, Universität Regensburg.
    • (1995)
    • Miller, S.1
  • 34
    • 0026628963 scopus 로고
    • Amino acid substitutions influencing intracellular protein folding pathways
    • Mitraki, A., and King. J. (1992). Amino acid substitutions influencing intracellular protein folding pathways. FEBS Lett. 307. 20-25.
    • (1992) FEBS Lett. , vol.307 , pp. 20-25
    • Mitraki, A.1    King, J.2
  • 35
    • 0025850262 scopus 로고
    • Global suppression of protein folding defects and inclusion body formation
    • Mitraki, A., Fane, B., Haase-Pettingell, C., Strutevant, J., and King, J. (1991). Global suppression of protein folding defects and inclusion body formation. Science 253, 54-58.
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Pettingell, C.3    Strutevant, J.4    King, J.5
  • 36
    • 0027321843 scopus 로고
    • Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro
    • Mitraki, A., Danner, M. King, J., and Seckler, R. (1993). Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. J. Biol. Chem. 268, 20071-20075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20071-20075
    • Mitraki, A.1    Danner, M.2    King, J.3    Seckler, R.4
  • 37
    • 0018816904 scopus 로고
    • Lipopolysaccharide Heterogeneity in Salmonella typhimurium analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis
    • Palva, E. T., and Mäkelä, H. (1980). Lipopolysaccharide Heterogeneity in Salmonella typhimurium analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Eur. J. Biochem. 707, 137-143.
    • (1980) Eur. J. Biochem. , vol.707 , pp. 137-143
    • Palva, E.T.1    Mäkelä, H.2
  • 38
    • 0028844306 scopus 로고
    • A left-handed parallel p helix in the structure of UDP-N-acetylglucosamine acyltrans-ferase
    • Raetz, C. R. H., and Roderick, L. (1995). A left-handed parallel p helix in the structure of UDP-N-acetylglucosamine acyltrans-ferase. Science 270, 997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, L.2
  • 39
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey, F. A., Heinz, R.X., Mandl., C., Kunz, C., and Harrison, S. C. (1995). The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375, 291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, R.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 40
    • 0024310169 scopus 로고
    • Characterization of bacteriophage P22 tailspike mutant proteins with altered endo-rhamnosidase and capsid assembly activities
    • Schwarz, J. J., and Berget, R.B. (1989). Characterization of bacteriophage P22 tailspike mutant proteins with altered endo-rhamnosidase and capsid assembly activities. J. Biol. Chem. 254, 20112-20119.
    • (1989) J. Biol. Chem. , vol.254 , pp. 20112-20119
    • Schwarz, J.J.1    Berget, R.B.2
  • 41
    • 0019429457 scopus 로고
    • Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein III. Inactive polypetide chains synthesized at 39°C
    • Smith, D. H., and King, J. (1981). Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein III. Inactive polypetide chains synthesized at 39°C. J. Mol. Biol. 145, 653-676.
    • (1981) J. Mol. Biol. , vol.145 , pp. 653-676
    • Smith, D.H.1    King, J.2
  • 42
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer
    • Steinbacher, S. Seckler, R., Miller, S., Steipe, B., Huber, R., and Reinemer, R (1994). Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, R.6
  • 43
    • 0029764093 scopus 로고    scopus 로고
    • Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors
    • Steinbacher, S., Baxa, U., Miller, S., Weintraub, A., Seckler, R., and Huber, R. (1996). Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc. Natl. Acad. Sci. USA 93, 10584-10588.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10584-10588
    • Steinbacher, S.1    Baxa, U.2    Miller, S.3    Weintraub, A.4    Seckler, R.5    Huber, R.6
  • 44
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 A., fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of 0-antigen recognition and cleavage
    • in press
    • Steinbacher, S., Miller, S., Baxa, U., Budisa, N., Weintraub, A., Seckler, R., and Huber, R. (1997). Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 A., fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of 0-antigen recognition and cleavage. J. Mol. Biol., in press.
    • (1997) J. Mol. Biol.
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Budisa, N.4    Weintraub, A.5    Seckler, R.6    Huber, R.7
  • 45
    • 0018569187 scopus 로고
    • Salmonella bacteriophage glycanases: endorhamnosidases of Salmonella typhimurium bacteriophages
    • Svenson, S. B., Lonngren, J., Carlin, N., and Lindberg, A. A. (1979). Salmonella bacteriophage glycanases: endorhamnosidases of Salmonella typhimurium bacteriophages. J. Virol. 32, 583-592.
    • (1979) J. Virol. , vol.32 , pp. 583-592
    • Svenson, S.B.1    Lonngren, J.2    Carlin, N.3    Lindberg, A.A.4
  • 46
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • Varghese, J. N., Laver, W. G., and Colman, R M. (1983). Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303, 35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, R.M.3
  • 47
    • 0011164677 scopus 로고
    • Heterogeneity in oligosaccharides from the O-polysaccharide chain of the lipopolysaccharide from Salmonella typhi 253Ty determined by fast atom bombardment mass spectrometry
    • Weintraub, A., Lindberg, A. A., Lipniunas, P., and Nilsson, B. (1988). Heterogeneity in oligosaccharides from the 0-polysaccharide chain of the lipopolysaccharide from Salmonella typhi 253Ty determined by fast atom bombardment mass spectrometry. Glycoconjugate J. 5, 207-213.
    • (1988) Glycoconjugate J. , vol.5 , pp. 207-213
    • Weintraub, A.1    Lindberg, A.A.2    Lipniunas, P.3    Nilsson, B.4
  • 48
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 49
    • 0028774724 scopus 로고
    • Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution
    • Xia, D., Henry, L. J., Gerard, R. D., and Deisenhofer, J. (1994). Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2, 1259-1270.
    • (1994) Structure , vol.2 , pp. 1259-1270
    • Xia, D.1    Henry, L.J.2    Gerard, R.D.3    Deisenhofer, J.4
  • 50
    • 0029257535 scopus 로고
    • The parallel P helix and other coiled folds
    • Yoder, M. D., and Jurnak, R. (1995). The parallel P helix and other coiled folds. FASEB J. 9, 335-342.
    • (1995) FASEB J. , vol.9 , pp. 335-342
    • Yoder, M.D.1    Jurnak, R.2
  • 51
    • 0027329090 scopus 로고
    • New domain motif: the structure of pectate lyase C. a secreted plant virulence factor
    • Yoder, M. D., Noel, T. K., and Jurnak, R. (1993). New domain motif: the structure of pectate lyase C. a secreted plant virulence factor. Science 260, 1503-1607.
    • (1993) Science , vol.260 , pp. 1503-1607
    • Yoder, M.D.1    Noel, T.K.2    Jurnak, R.3


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