메뉴 건너뛰기




Volumn 11, Issue 1, 2003, Pages 75-85

Metal-free and Ca2+-bound structures of a multidomain EF-hand protein, CBP40, from the lower eukaryote Physarum polycephalum

Author keywords

Calcium binding protein 40; Calcium binding proteins; Crystal structure; EF hand; Physarum polycephalum

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM BINDING PROTEIN 40; CALCIUM ION; EF HAND PROTEIN; METAL; PROTEIN; UNCLASSIFIED DRUG; CALCIUM; CALMODULIN; CALPAIN; CBP40 PROTEIN, PHYSARUM; PROTOZOAL PROTEIN;

EID: 0642284474     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00932-2     Document Type: Article
Times cited : (9)

References (48)
  • 2
    • 0012371177 scopus 로고
    • Screw-mechanical models related to cytoplasmic streaming
    • Jarosch R. Screw-mechanical models related to cytoplasmic streaming. Protoplasma Suppl. 1:1988;15-26.
    • (1988) Protoplasma Suppl. , vol.1 , pp. 15-26
    • Jarosch, R.1
  • 3
    • 0000652525 scopus 로고
    • Physical and chemical basis of cytoplasmic streaming
    • Kamiya N. Physical and chemical basis of cytoplasmic streaming. Annu. Rev. Plant Physiol. 32:1981;205-236.
    • (1981) Annu. Rev. Plant Physiol. , vol.32 , pp. 205-236
    • Kamiya, N.1
  • 4
    • 0032491610 scopus 로고    scopus 로고
    • Characterization of 101-kDa transglutaminase from Physarum polycephalum and identification of LAV1-2 as substrate
    • Mottahedeh J., Marsh R. Characterization of 101-kDa transglutaminase from Physarum polycephalum and identification of LAV1-2 as substrate. J. Biol. Chem. 273:1998;29888-29895.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29888-29895
    • Mottahedeh, J.1    Marsh, R.2
  • 6
    • 0025894078 scopus 로고
    • Purification of a novel Ca-binding protein that inhibits myosin light chain kinase activity in lower eukaryote Physarum polycephalum
    • Okagaki T., Ishikawa R., Kohama K. Purification of a novel Ca-binding protein that inhibits myosin light chain kinase activity in lower eukaryote Physarum polycephalum. Biochem. Biophys. Res. Commun. 176:1991;564-570.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 564-570
    • Okagaki, T.1    Ishikawa, R.2    Kohama, K.3
  • 7
    • 0022870997 scopus 로고
    • Molecular cloning of stage specific mRNAs from amoebae and plasmodia of Physarum polycephalum
    • Pallota D., Laroche A., Terrier A. Molecular cloning of stage specific mRNAs from amoebae and plasmodia of Physarum polycephalum. Biochem. Cell Biol. 64:1986;1294-1302.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 1294-1302
    • Pallota, D.1    Laroche, A.2    Terrier, A.3
  • 8
    • 0024829783 scopus 로고
    • The nucleotide sequence of a developmentally regulated cDNA from Physarum polycephalum
    • Laroche A., Lemieux G., Pallotta D. The nucleotide sequence of a developmentally regulated cDNA from Physarum polycephalum. Nucleic Acids Res. 17:1989;10502.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10502
    • Laroche, A.1    Lemieux, G.2    Pallotta, D.3
  • 9
    • 0034603789 scopus 로고    scopus 로고
    • Calcium binding properties of recombinant calcium binding protein 40, a major calcium binding protein of lower eukaryote Physarum polycephalum
    • Nakamura A., Okagaki T., Takagi T., Nakashima K., Yazawa M., Kohama K. Calcium binding properties of recombinant calcium binding protein 40, a major calcium binding protein of lower eukaryote Physarum polycephalum. Biochemistry. 39:2000;3827-3834.
    • (2000) Biochemistry , vol.39 , pp. 3827-3834
    • Nakamura, A.1    Okagaki, T.2    Takagi, T.3    Nakashima, K.4    Yazawa, M.5    Kohama, K.6
  • 11
    • 0026012519 scopus 로고
    • +2-regulation of ATP-dependent interaction between actin and myosin of a lower eukaryote, Physarum polycephalum
    • +2-regulation of ATP-dependent interaction between actin and myosin of a lower eukaryote, Physarum polycephalum. J. Biochem. 110:1991;508-513.
    • (1991) J. Biochem. , vol.110 , pp. 508-513
    • Kohama, K.1    Kohno, T.2    Okagaki, T.3    Shimmen, T.4
  • 12
    • 0033004788 scopus 로고    scopus 로고
    • Calcium regulation of the actin-myosin interaction of Physarum polycephalum
    • Nakamura A., Kohama K. Calcium regulation of the actin-myosin interaction of Physarum polycephalum. Int. Rev. Cytol. 191:1999;53-98.
    • (1999) Int. Rev. Cytol. , vol.191 , pp. 53-98
    • Nakamura, A.1    Kohama, K.2
  • 13
    • 0035853291 scopus 로고    scopus 로고
    • Socket: A program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw J., Woolfson D.N. Socket. a program for identifying and analysing coiled-coil motifs within protein structures J. Mol. Biol. 307:2001;1427-1450.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 14
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • Ruoslahti E., Pierschbacher M.D. Arg-Gly-Asp. a versatile cell recognition signal Cell. 44:1986;517-518.
    • (1986) Cell , vol.44 , pp. 517-518
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 15
    • 0011832293 scopus 로고
    • Identification and synthesis of a recognition signal for attachment of glycosaminoglycans to proteins
    • Bourdon M.A., Krusius T., Campbell S., Schwartz N.B., Ruoslachti E. Identification and synthesis of a recognition signal for attachment of glycosaminoglycans to proteins. Proc. Natl. Acad. Sci. USA. 84:1987;3194-3198.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3194-3198
    • Bourdon, M.A.1    Krusius, T.2    Campbell, S.3    Schwartz, N.B.4    Ruoslachti, E.5
  • 17
  • 18
    • 0033573028 scopus 로고    scopus 로고
    • Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation
    • Hosfield C.M., Elce J.S., Davies P.L., Jia Z. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18:1999;6880-6889.
    • (1999) EMBO J. , vol.18 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 20
    • 0034725530 scopus 로고    scopus 로고
    • Crystal structure of human grancalcin, a member of the penta-EF-hand protein family
    • Jia J., Han Q., Borregaard N., Lollike K., Cygler M. Crystal structure of human grancalcin, a member of the penta-EF-hand protein family. J. Mol. Biol. 300:2000;1271-1281.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1271-1281
    • Jia, J.1    Han, Q.2    Borregaard, N.3    Lollike, K.4    Cygler, M.5
  • 22
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu Y.S., Bugg C.E., Cook W.J. Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204:1988;191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 24
    • 0032820524 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a 40 kDa calcium binding protein specifically expressed in plasmodia of Physarum polycephalum
    • Iwasaki W., Sasaki H., Nakamura A., Kohama K., Tanokura M. Crystallization and preliminary X-ray diffraction studies of a 40 kDa calcium binding protein specifically expressed in plasmodia of Physarum polycephalum. J. Biochem. 126:1999;7-9.
    • (1999) J. Biochem. , vol.126 , pp. 7-9
    • Iwasaki, W.1    Sasaki, H.2    Nakamura, A.3    Kohama, K.4    Tanokura, M.5
  • 25
    • 0030995856 scopus 로고    scopus 로고
    • Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains of BM-40
    • Hohenester E., Maurer P., Timpl R. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains of BM-40. EMBO J. 16:1997;3778-3786.
    • (1997) EMBO J. , vol.16 , pp. 3778-3786
    • Hohenester, E.1    Maurer, P.2    Timpl, R.3
  • 26
    • 0021129756 scopus 로고
    • 2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates
    • 2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates. J. Biol. Chem. 259:1984;10949-10955.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10949-10955
    • Olwin, B.B.1    Edelman, A.M.2    Krebs, E.G.3    Storm, D.R.4
  • 27
    • 0028222312 scopus 로고
    • Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B
    • Stemmer P.M., Klee C.B. Dual calcium ion regulation of calcineurin by calmodulin and calcineurin B. Biochemistry. 33:1994;6859-6866.
    • (1994) Biochemistry , vol.33 , pp. 6859-6866
    • Stemmer, P.M.1    Klee, C.B.2
  • 29
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 256:1992;632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 30
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador W.E., Means A.R., Quiocho F.A. Target enzyme recognition by calmodulin. 2.4 Å structure of a calmodulin-peptide complex Science. 257:1992;1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 31
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structure
    • Meador W.E., Means A.R., Quiocho F. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structure. Science. 262:1993;1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.3
  • 33
    • 0017280108 scopus 로고
    • Oscillations of calcium ion concentrations in Physarum polycephalum
    • Ridgway E.B., Durham A.C.H. Oscillations of calcium ion concentrations in Physarum polycephalum. J. Cell Biol. 69:1976;223-226.
    • (1976) J. Cell Biol. , vol.69 , pp. 223-226
    • Ridgway, E.B.1    Durham, A.C.H.2
  • 36
    • 0031686336 scopus 로고    scopus 로고
    • 9k in the apo and singly and doubly calcium-loaded states
    • 9k in the apo and singly and doubly calcium-loaded states. Proteins. 33:1998;265-284.
    • (1998) Proteins , vol.33 , pp. 265-284
    • Marchand, S.1    Roux, B.2
  • 37
    • 18844478967 scopus 로고    scopus 로고
    • Backbone and methyl dynamics of the regulatory domain of tropoin C: Anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity
    • Gagné S.M., Tsuda S., Spyracopoulus L., Kay L.E., Sykes B.D. Backbone and methyl dynamics of the regulatory domain of tropoin C. anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity J. Mol. Biol. 278:1998;667-686.
    • (1998) J. Mol. Biol. , vol.278 , pp. 667-686
    • Gagné, S.M.1    Tsuda, S.2    Spyracopoulus, L.3    Kay, L.E.4    Sykes, B.D.5
  • 39
    • 0035947576 scopus 로고    scopus 로고
    • Biochemical characterization of the penta-EF-hand protein grancalcin and identification of L-plastin as a binding partner
    • Lollike K., Johnsen A.H., Durussel I., Borregaard N., Cox J.A. Biochemical characterization of the penta-EF-hand protein grancalcin and identification of L-plastin as a binding partner. J. Biol. Chem. 276:2001;17762-17769.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17762-17769
    • Lollike, K.1    Johnsen, A.H.2    Durussel, I.3    Borregaard, N.4    Cox, J.A.5
  • 40
    • 0026751153 scopus 로고
    • Ca(2+)-dependent translocation of cytosolic proteins to isolated granule subpopulations and plasma membrane from human neutrophils
    • Borregaard N., Kjeldsen L., Lollike K., Sengelov H. Ca(2+)-dependent translocation of cytosolic proteins to isolated granule subpopulations and plasma membrane from human neutrophils. FEBS Lett. 304:1992;195-197.
    • (1992) FEBS Lett. , vol.304 , pp. 195-197
    • Borregaard, N.1    Kjeldsen, L.2    Lollike, K.3    Sengelov, H.4
  • 42
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone
    • Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms. implications for the biogenesis of topaquinone Biochemistry. 36:1997;16116-16133.
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Matsunami, H.5    McIntire, W.S.6    Ruggiero, C.E.7    Tanizawa, K.8    Yamaguchi, H.9
  • 43
    • 0012443747 scopus 로고
    • Isomorphous replacement and anomalous scattering
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington, UK: SERC Daresbury Laboratory. 55-62.pp
    • Otwinowski Z. Isomorphous replacement and anomalous scattering. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend. Data Collection and Processing:1993;SERC Daresbury Laboratory, Warrington, UK. 55-62.pp.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing
    • Otwinowski, Z.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 45
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and for locating erros in these model
    • Jones A.T., Zou J.-Y., Cowtan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and for locating erros in these model. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, A.T.1    Zou, J.-Y.2    Cowtan, S.W.3    Kjeldgaard, M.4
  • 48
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.