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Volumn 37, Issue 4, 2004, Pages 733-745

Structural-functional analysis of the oligomeric protein R-phycoerythrin

Author keywords

Anchor points; Interaction surfaces; Leyx; Spectroscopic sensitivity; Stability

Indexed keywords

ARGININE; ASPARTIC ACID; CARBOXYLIC ACID; DIMER; GLUTAMINE; HYDROGEN; LYSINE; MONOMER; NITROGEN; OLIGOMER; PHYCOBILIPROTEIN; PHYCOERYTHRIN; PYRROLE DERIVATIVE; R PHYCOERYTHRIN; UNCLASSIFIED DRUG;

EID: 9444284434     PISSN: 07169760     EISSN: None     Source Type: Journal    
DOI: 10.4067/S0716-97602004000500003     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 0035850751 scopus 로고    scopus 로고
    • Structure of C-phycocyanin from the thermophylic cyanobacterium Synechococcus vulcanus at 2.5Å: Structural implications for thermal stability in phycobilisome assembly
    • ADIR N, DOBROVETSKY E, LERNER N (2001) Structure of C-phycocyanin from the thermophylic cyanobacterium Synechococcus vulcanus at 2.5Å: Structural implications for thermal stability in phycobilisome assembly. J Mol Biol 313: 71-81
    • (2001) J. Mol. Biol. , vol.313 , pp. 71-81
    • Adir, N.1    Dobrovetsky, E.2    Lerner, N.3
  • 3
    • 0029037179 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3Å resolution
    • BREJC K, FICNER R, HUBER R, STEINBACHER S (1995) Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3Å resolution. J Mol Biol 249: 424-440
    • (1995) J. Mol. Biol. , vol.249 , pp. 424-440
    • Brejc, K.1    Ficner, R.2    Huber, R.3    Steinbacher, S.4
  • 4
    • 0006674490 scopus 로고    scopus 로고
    • Characterization of phycobiliproteins present in Gracilaria chilensis
    • BUNSTER M, TELLEZ J, CANDIA A (1997) Characterization of phycobiliproteins present in Gracilaria chilensis. Bol Soc Chil Quím 42: 449-455
    • (1997) Bol. Soc. Chil. Quím. , vol.42 , pp. 449-455
    • Bunster, M.1    Tellez, J.2    Candia, A.3
  • 6
    • 0030580059 scopus 로고    scopus 로고
    • Crystal structure of R-phycoerythrin from Polisiphonia urceolata at 2.0Å resolution
    • CHANG WR, JIANG T, WANG ZL, YANG ZX, LIANG DC (1996) Crystal structure of R-phycoerythrin from Polisiphonia urceolata at 2.0Å resolution. J Mol Biol 262: 721-731
    • (1996) J. Mol. Biol. , vol.262 , pp. 721-731
    • Chang, W.R.1    Jiang, T.2    Wang, Z.L.3    Yang, Z.X.4    Liang, D.C.5
  • 7
    • 9444292949 scopus 로고    scopus 로고
    • Resolución de la estructura terciaria de R-ficoeritrina de Gracilaria chilensis. Tesis para optar al grado de Doctor en Ciencias Biológicas. Universidad de Concepción
    • CONTRERAS-MARTEL C (2000) Resolución de la estructura terciaria de R-ficoeritrina de Gracilaria chilensis. Tesis para optar al grado de Doctor en Ciencias Biológicas. Universidad de Concepción. pp: 100-104
    • (2000) , pp. 100-104
    • Contreras-Martel, C.1
  • 9
    • 0025967561 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66Å resolution
    • DUERRING M, SCHMIDT G, HUBER R (1991) Isolation, crystallization, crystal structure analysis and refinement of constitutive C-phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66Å resolution. J Mol Biol 217: 577-592
    • (1991) J. Mol. Biol. , vol.217 , pp. 577-592
    • Duerring, M.1    Schmidt, G.2    Huber, R.3
  • 10
    • 0022748485 scopus 로고
    • Linker polypeptides from the cyanobacterium Mastigoclaudus laminosus. II Amino acid sequences and function
    • FLUGISTALLER P, SUTER F, ZUBER H (1986) Linker polypeptides from the cyanobacterium Mastigoclaudus laminosus. II Amino acid sequences and function. Biol Chem Hoppe-Seyler 367: 615-626
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 615-626
    • Flugistaller, P.1    Suter, F.2    Zuber, H.3
  • 11
    • 0017238005 scopus 로고
    • Further evidence for a phycobilisome model from selective dissociation, fluorescence emission, immunoprecipitation and electron microscopy
    • GANTT E, LIPSCHUTZ CA, ZILENKAS B (1976) Further evidence for a phycobilisome model from selective dissociation, fluorescence emission, immunoprecipitation and electron microscopy. BB Acta 430: 375-378
    • (1976) BB Acta , vol.430 , pp. 375-378
    • Gantt, E.1    Lipschutz, C.A.2    Zilenkas, B.3
  • 12
    • 0001073978 scopus 로고
    • A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites
    • GERSTEIN M (1992) A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites. Acta Cryst A 48: 271-276
    • (1992) Acta Cryst. A. , vol.48 , pp. 271-276
    • Gerstein, M.1
  • 13
    • 0024961673 scopus 로고
    • Light guides. Directional energy transfer in a photosynthetic antenna
    • GLAZER AN (1989) Light guides. Directional energy transfer in a photosynthetic antenna. J Biol Chem 264: 1-4
    • (1989) J. Biol. Chem. , vol.264 , pp. 1-4
    • Glazer, A.N.1
  • 14
    • 0034901819 scopus 로고    scopus 로고
    • Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome
    • JIANG T, ZHANG JP, CHANG WR, LIANG DC (2001) Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome. Biophys J 81: 1171-1179
    • (2001) Biophys. J. , vol.81 , pp. 1171-1179
    • Jiang, T.1    Zhang, J.P.2    Chang, W.R.3    Liang, D.C.4
  • 16
    • 33744811377 scopus 로고
    • The theory of the hydrogen bond
    • KOLLMAN PA, ALLEN LC (1972) The theory of the hydrogen bond. Chem Rev 72: 283-303
    • (1972) Chem. Rev. , vol.72 , pp. 283-303
    • Kollman, P.A.1    Allen, L.C.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins of bacteriophage T4
    • LAEMMLI UK (1970) Cleavage of structural proteins of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • MACDONALD I, THORNTON J (1994) Satisfying hydrogen bonding potential in proteins. J Mol Biol 238: 777-793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • Macdonald, I.1    Thornton, J.2
  • 19
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • NAKAMURA H (1996) Roles of electrostatic interaction in proteins. Q Rev Biophys 29: 1-90
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 20
    • 0009388594 scopus 로고    scopus 로고
    • Quantitation of proteins separated by electrophoresis using Commassie brilliant blue
    • WALKER JM (ed) Totowa, NJ: Humana Press Inc
    • NEUMANN U (1996) Quantitation of proteins separated by electrophoresis using Commassie brilliant blue. In: WALKER JM (ed) The Proteins Protocols Handbook. Totowa, NJ: Humana Press Inc. pp: 173-178
    • (1996) The Proteins Protocols Handbook , pp. 173-178
    • Neumann, U.1
  • 21
    • 0033573901 scopus 로고    scopus 로고
    • Structural analysis at 2.2Å of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex AP.LC7.8 from phycobilisomes from Mastigoclaudus laminosus
    • REUTER W, WIEGAND G, HUBER R, THAN ME (1999) Structural analysis at 2.2Å of orthorhombic crystals presents the asymmetry of the allophycocyanin-linker complex AP.LC7.8 from phycobilisomes from Mastigoclaudus laminosus. Proc Natl Acad Sci USA 96: 1363-1368
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1363-1368
    • Reuter, W.1    Wiegand, G.2    Huber, R.3    Than, M.E.4
  • 22
    • 0033563668 scopus 로고    scopus 로고
    • Crystal Structure of a phycourobilin-containing phycoerythrin at 1.9Å resolution
    • RITTER S, HILLER RG, WRENCH PM, WELTE W DIEDERICH K (1999) Crystal Structure of a phycourobilin-containing phycoerythrin at 1.9Å resolution. J Struct Biol 126: 86-97
    • (1999) J. Struct. Biol. , vol.126 , pp. 86-97
    • Ritter, S.1    Hiller, R.G.2    Wrench, P.M.3    Welte, W.4    Diederich, K.5
  • 23
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability and the hydrophobic interaction
    • SCHELLMAN JA (1997) Temperature, stability and the hydrophobic interaction. Biophys J 73: 2960-2964
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 24
    • 0023053285 scopus 로고
    • Crystal structure analysis and refinement at 2.5Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum cuadruplicatum
    • SCHIRMER T, HUBER R, SCHNEIDER M, BODE W, MILLER M, HACKERT M (1986) Crystal structure analysis and refinement at 2.5Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum cuadruplicatum. J Mol Biol 188: 651-676
    • (1986) J. Mol. Biol. , vol.188 , pp. 651-676
    • Schirmer, T.1    Huber, R.2    Schneider, M.3    Bode, W.4    Miller, M.5    Hackert, M.6
  • 25
    • 0023645201 scopus 로고
    • Refined three dimensional structure of two cyanobacterial C-phycocyanins at 2.1 and 2.5Å resolution
    • SCHIRMER T, BODE W, HUBER R (1987) Refined three dimensional structure of two cyanobacterial C-phycocyanins at 2.1 and 2.5Å resolution. J Mol Biol 196: 677-645
    • (1987) J. Mol. Biol. , vol.196 , pp. 645-677
    • Schirmer, T.1    Bode, W.2    Huber, R.3
  • 26
    • 0024989528 scopus 로고
    • Separation of phycobiliproteins subunits by reverse phase high pressure liquid chromatography
    • SWANSON RV, GLAZER AN (1990) Separation of phycobiliproteins subunits by reverse phase high pressure liquid chromatography. Anal Biochem 88: 295-299
    • (1990) Anal. Biochem. , vol.88 , pp. 295-299
    • Swanson, R.V.1    Glazer, A.N.2
  • 27
    • 0037197254 scopus 로고    scopus 로고
    • A novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • TSODIKOV OV, RECORD MT JR, SERGEEV YV (2002) A novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J Comp Biol 23: 600-609
    • (2002) J. Comp. Biol. , vol.23 , pp. 600-609
    • Tsodikov, O.V.1    Record, M.T.J.R.2    Sergeev, Y.V.3
  • 28
    • 0031737482 scopus 로고    scopus 로고
    • Bilin deletions and subunit stability in cyanobacterial light harvesting proteins
    • TOOLE CM, PLANK TL, GROSSMAN AR, ANDERSON LK (1998) Bilin deletions and subunit stability in cyanobacterial light harvesting proteins. Mol Microbiol 30: 475-486
    • (1998) Mol. Microbiol. , vol.30 , pp. 475-486
    • Toole, C.M.1    Plank, T.L.2    Grossman, A.R.3    Anderson, L.K.4
  • 29
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • TSAI CJ, LIN SL, WOLFSON HJ, NUSSINOV R (1997) Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect. Protein Sci 6: 53-64
    • (1997) Protein. Sci. , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.