메뉴 건너뛰기




Volumn 17, Issue 4, 1998, Pages 977-984

Synapsin I is structurally similar to ATP-utilizing enzymes

Author keywords

ATP binding; Ca2+ binding; Crystal structure; Structural similarity; Synaptic vesicle proteins

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; MAGNESIUM; SYNAPSIN I;

EID: 0032481344     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.4.977     Document Type: Article
Times cited : (114)

References (39)
  • 2
    • 0023201681 scopus 로고
    • Synapsin I bundles F-actin in a phosphorylation-dependent manner
    • Bähler, M. and Greengard, P. (1987) Synapsin I bundles F-actin in a phosphorylation-dependent manner. Nature, 326, 704-707.
    • (1987) Nature , vol.326 , pp. 704-707
    • Bähler, M.1    Greengard, P.2
  • 3
    • 0021814766 scopus 로고
    • Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1
    • Baines, A.J. and Bennett, V. (1985) Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1. Nature, 315, 410-413.
    • (1985) Nature , vol.315 , pp. 410-413
    • Baines, A.J.1    Bennett, V.2
  • 4
    • 0022630780 scopus 로고
    • Synapsin I is a microtubule-binding protein
    • Baines, A.J. and Bennett, V. (1986) Synapsin I is a microtubule-binding protein. Nature, 319, 145-147.
    • (1986) Nature , vol.319 , pp. 145-147
    • Baines, A.J.1    Bennett, V.2
  • 7
    • 0028103275 scopus 로고
    • CCP4
    • Collaborative Computational Project Number 4, (1994) CCP4. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 8
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. and Main, P. (1996) Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr., D52, 43-48.
    • (1996) Acta Crystallogr , vol.D52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 9
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997) An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graph., 15, 133-138.
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 10
    • 0027945446 scopus 로고
    • Molecular tuning of ion binding to calcium signaling proteins
    • Falke, J.J., Drake, S.K., Hazard, A.L. and Peersen, O.B. (1994) Molecular tuning of ion binding to calcium signaling proteins. Q. Rev. Biophys., 21, 219-290.
    • (1994) Q. Rev. Biophys. , vol.21 , pp. 219-290
    • Falke, J.J.1    Drake, S.K.2    Hazard, A.L.3    Peersen, O.B.4
  • 11
    • 0028151598 scopus 로고
    • Vancomycin resistance: Structure of D-alanine:D-alanine ligase at 2.3 Å resolution
    • Fan, C., Moews, P.C., Walsh, C.T. and Knox, J.R. (1994) Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 Å resolution. Science, 266, 439-143.
    • (1994) Science , vol.266 , pp. 439-1143
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 12
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
    • Flaherty, K.M., Wilbanks, S.M., DeLuca-Flaherty, C. and McKay, D.B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J. Biol. Chem., 269, 12899-12907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    DeLuca-Flaherty, C.3    McKay, D.B.4
  • 13
    • 0023296231 scopus 로고
    • Neuronal phosphoproteins
    • Greengard, P. (1987) Neuronal phosphoproteins. Mol. Neurobiol., 1, 81-119.
    • (1987) Mol. Neurobiol. , vol.1 , pp. 81-119
    • Greengard, P.1
  • 14
    • 0025818538 scopus 로고
    • 2+dependent interaction of calmodulin with the head domain of synapsin I
    • 2+dependent interaction of calmodulin with the head domain of synapsin I. Biochem. J., 275, 93-97.
    • (1991) Biochem. J. , vol.275 , pp. 93-97
    • Hayes, N.V.1    Bennett, A.F.2    Baines, A.J.3
  • 16
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 17
    • 0028080836 scopus 로고
    • Annexin VI binds to a synaptic vesicle protein, synapsin I
    • Inui, M., Watanabe, T. and Sobue, K. (1994) Annexin VI binds to a synaptic vesicle protein, synapsin I. J. Neurochem., 63, 1917-1923.
    • (1994) J. Neurochem. , vol.63 , pp. 1917-1923
    • Inui, M.1    Watanabe, T.2    Sobue, K.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y. Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr., A47, 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0025807843 scopus 로고
    • Cytosolic rat brain synapsin I is a diacylglycerol kinase
    • Kahn, D.W. and Besterman, J.M. (1991) Cytosolic rat brain synapsin I is a diacylglycerol kinase. Proc. Natl Acad. Sci. USA, 88, 6137-6141.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6137-6141
    • Kahn, D.W.1    Besterman, J.M.2
  • 20
    • 9244254745 scopus 로고    scopus 로고
    • Invertebrate synapsins: A single gene codes for several isoforms in Drosophila
    • Klagges, B.R.E. et al. (1996) Invertebrate synapsins: a single gene codes for several isoforms in Drosophila. J. Neurosci., 16, 3154-3165.
    • (1996) J. Neurosci. , vol.16 , pp. 3154-3165
    • Klagges, B.R.E.1
  • 21
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots structures
    • Kraulis, P.J. (1991) Molscript: a program to produce both detailed and schematic plots structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0030447825 scopus 로고    scopus 로고
    • Crystal structure of glutathione synthetase at optimal pH: Domain architecture and structural similarity with other proteins
    • Matsuda, K., Mizuguchi, K., Nishioka, T., Kato, H., Go, N. and Oda, J. (1996) Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Protein Eng., 9, 1083-1092.
    • (1996) Protein Eng , vol.9 , pp. 1083-1092
    • Matsuda, K.1    Mizuguchi, K.2    Nishioka, T.3    Kato, H.4    Go, N.5    Oda, J.6
  • 24
    • 0026608008 scopus 로고
    • Acidic calmodulin-binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I
    • Mizutani, A., Tokumitsu, H. and Hidaka, H. (1992) Acidic calmodulin-binding protein, ACAMP-81, is MARCKS protein interacting with synapsin I. Biochem. Biophys. Res. Commun., 182, 1395-1401.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1395-1401
    • Mizutani, A.1    Tokumitsu, H.2    Hidaka, H.3
  • 25
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol., 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0023584584 scopus 로고    scopus 로고
    • Synapsin I: An actin-bundling protein under phosphorylation control
    • Petrucci, T.C. and Morrow, J. (1997) Synapsin I: an actin-bundling protein under phosphorylation control. J. Cell Biol., 105, 1355-1363.
    • (1997) J. Cell Biol. , vol.105 , pp. 1355-1363
    • Petrucci, T.C.1    Morrow, J.2
  • 31
    • 0031569356 scopus 로고    scopus 로고
    • Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
    • Sriram, M., Osipiuk, J., Freeman, B.C., Morimoto, R.I. and Joachimiak, A. (1997) Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure, 5, 403-414.
    • (1997) Structure , vol.5 , pp. 403-414
    • Sriram, M.1    Osipiuk, J.2    Freeman, B.C.3    Morimoto, R.I.4    Joachimiak, A.5
  • 33
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. (1995) The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature, 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 34
    • 0024461324 scopus 로고
    • Synapsins: Mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins
    • Südhof, T.C. et al. (1989) Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins. Science, 245, 1474-1480.
    • (1989) Science , vol.245 , pp. 1474-1480
    • Südhof, T.C.1
  • 35
    • 0026562680 scopus 로고
    • Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: The loop and arginine 233 are critical for the catalytic reaction
    • Tanaka, T., Kato, H., Nishioka, T. and Oda, J. (1992) Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction. Biochemistry, 31, 2259-2265.
    • (1992) Biochemistry , vol.31 , pp. 2259-2265
    • Tanaka, T.1    Kato, H.2    Nishioka, T.3    Oda, J.4
  • 36
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop, G.L., Rayment, I. and Holden, H.M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry, 33, 10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 37
    • 0030854182 scopus 로고    scopus 로고
    • Identification, expression, and crystallization of the proteaseresistant conserved domain of synapsin I
    • Wang, C.-R., Esser, L., Smagula, C.S., Südhof, T.C. and DeisenhoferJ. (1997) Identification, expression, and crystallization of the proteaseresistant conserved domain of synapsin I. Protein Sci., 6, 2264-2267.
    • (1997) Protein Sci , vol.6 , pp. 2264-2267
    • Wang, C.-R.1    Esser, L.2    Smagula, C.S.3    Südhof, T.C.4    Deisenhofer, J.5
  • 38
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution
    • Wolodko, W.T., Fraser, M.E., James, M.N.G. and Bridger, W.A. (1994) The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution. J. Biol. Chem., 269, 10883-10890.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.G.3    Bridger, W.A.4
  • 39
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J. and Katsube, Y. (1993) Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution. J. Mol. Biol., 229, 1083-1100.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.