메뉴 건너뛰기




Volumn 346, Issue 5, 2005, Pages 1351-1366

Structure of a trapped intermediate of calmodulin: Calcium regulation of EF-hand proteins from a new perspective

Author keywords

Ca2+ binding; Calmodulin; Disulfide crosslinking; EF hand; X ray crystallography

Indexed keywords

CALCIUM ION; CALMODULIN; CALMODULIN 41; CALMODULIN 75; COORDINATION COMPOUND; DISULFIDE; GLUTAMIC ACID; LIGAND; MUTANT PROTEIN; SOLVENT; TROPONIN C; UNCLASSIFIED DRUG;

EID: 13844272482     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.004     Document Type: Article
Times cited : (65)

References (58)
  • 1
    • 0024196034 scopus 로고
    • Molecular mechanisms of action of calmodulin
    • A.R. Means Molecular mechanisms of action of calmodulin Recent Prog. Horm. Res. 44 1988 223 262
    • (1988) Recent Prog. Horm. Res. , vol.44 , pp. 223-262
    • Means, A.R.1
  • 2
    • 0023471689 scopus 로고
    • Calcium coordination and the calmodulin fold: Divergent versus convergent evolution
    • R.H. Kretsinger Calcium coordination and the calmodulin fold: divergent versus convergent evolution Cold Spring Harbor Symp. Quant. Biol. 52 1987 499 510
    • (1987) Cold Spring Harbor Symp. Quant. Biol. , vol.52 , pp. 499-510
    • Kretsinger, R.H.1
  • 4
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Y.S. Babu, C.E. Bugg, and W.J. Cook 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
  • 7
    • 0025719432 scopus 로고
    • Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution
    • D.A. Taylor, J.S. Sack, J.F. Maune, K. Beckingham, and F.A. Quiocho Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution J. Biol. Chem. 266 1991 21375 21380
    • (1991) J. Biol. Chem. , vol.266 , pp. 21375-21380
    • Taylor, D.A.1    Sack, J.S.2    Maune, J.F.3    Beckingham, K.4    Quiocho, F.A.5
  • 8
    • 0034257929 scopus 로고    scopus 로고
    • 2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity
    • 2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity J. Mol. Biol. 301 2000 1237 1256
    • (2000) J. Mol. Biol. , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2
  • 9
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • N.C.J. Strynadka, and M.N.G. James Crystal structures of the helix-loop-helix calcium-binding proteins Annu. Rev. Biochem. 58 1989 951 998
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 11
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • M. Zhang, T. Tanaka, and M. Ikura Calcium-induced conformational transition revealed by the solution structure of apo calmodulin Nature Struct. Biol. 2 1995 758 767
    • (1995) Nature Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 12
    • 2342513320 scopus 로고    scopus 로고
    • Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex
    • M.A. Schumacher, M. Crum, and M.C. Miller Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex Structure (Camb) 12 2004 849 860
    • (2004) Structure (Camb) , vol.12 , pp. 849-860
    • Schumacher, M.A.1    Crum, M.2    Miller, M.C.3
  • 13
    • 0022931544 scopus 로고
    • 2+-induced conformational transition of troponin C a trigger for muscle contraction
    • 2+-induced conformational transition of troponin C A trigger for muscle contraction J. Biol. Chem. 261 1986 2638 2644
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.3
  • 14
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • C.L. Drum, S.Z. Yan, J. Bard, Y.Q. Shen, D. Lu, and S. Soelaiman Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin Nature 415 2002 396 402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5    Soelaiman, S.6
  • 16
    • 0030936958 scopus 로고    scopus 로고
    • Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins
    • S.M. Gagne, M.X. Li, and B.D. Sykes Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins Biochemistry 36 1997 4386 4392
    • (1997) Biochemistry , vol.36 , pp. 4386-4392
    • Gagne, S.M.1    Li, M.X.2    Sykes, B.D.3
  • 19
    • 0025736561 scopus 로고
    • 2+-induced conformational changes
    • 2+-induced conformational changes J. Biol. Chem. 266 1991 6027 6030
    • (1991) J. Biol. Chem. , vol.266 , pp. 6027-6030
    • Beckingham, K.1
  • 21
    • 0019865659 scopus 로고
    • Structure of vitamin D-dependent calcium-binding protein from bovine intestine
    • D.M.E. Szebenyi, S.K. Obendorf, and K. Moffat Structure of vitamin D-dependent calcium-binding protein from bovine intestine Nature 294 1981 327 332
    • (1981) Nature , vol.294 , pp. 327-332
    • Szebenyi, D.M.E.1    Obendorf, S.K.2    Moffat, K.3
  • 23
    • 0029665077 scopus 로고    scopus 로고
    • 2+-induced conformational transitions in calmodulin with disulfide bonds
    • 2+- induced conformational transitions in calmodulin with disulfide bonds J. Biol. Chem. 271 1996 7479 7483
    • (1996) J. Biol. Chem. , vol.271 , pp. 7479-7483
    • Tan, R.Y.1    Mabuchi, Y.2    Grabarek, Z.3
  • 24
    • 0029931376 scopus 로고    scopus 로고
    • 2+-induced conformational transition in the C-terminal domain of calmodulin
    • 2+-induced conformational transition in the C-terminal domain of calmodulin J. Biol. Chem. 271 1996 11284 11290
    • (1996) J. Biol. Chem. , vol.271 , pp. 11284-11290
    • Meyer, D.F.1    Mabuchi, Y.2    Grabarek, Z.3
  • 25
    • 0025271923 scopus 로고
    • Inhibition of mutant troponin C activity by an intra-domain disulphide bond
    • Z. Grabarek, R.Y. Tan, J. Wang, T. Tao, and J. Gergely Inhibition of mutant troponin C activity by an intra-domain disulphide bond Nature 345 1990 132 135
    • (1990) Nature , vol.345 , pp. 132-135
    • Grabarek, Z.1    Tan, R.Y.2    Wang, J.3    Tao, T.4    Gergely, J.5
  • 26
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • O. Herzberg, and M.N. James Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution Nature 313 1985 653 659
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.2
  • 28
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • R. Soudhamini, N. Srinivasan, B. Shoichet, D.V. Santi, C. Ramakrishnan, and P. Balaram Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis Protein Eng. 3 1989 95 103
    • (1989) Protein Eng. , vol.3 , pp. 95-103
    • Soudhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 29
    • 0027203053 scopus 로고
    • Kinetic control of Ca(II) signaling: Tuning the ion dissociation rates of EF-hand Ca(II) binding sites
    • M. Renner, M.A. Danielson, and J.J. Falke Kinetic control of Ca(II) signaling: tuning the ion dissociation rates of EF-hand Ca(II) binding sites Proc. Natl Acad. Sci. USA 90 1993 6493 6497
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6493-6497
    • Renner, M.1    Danielson, M.A.2    Falke, J.J.3
  • 32
    • 0025993048 scopus 로고
    • Stabilization by a disulfide bond of the N-terminal domain of a mutant troponin C (TnC48/82)
    • N.B. Gusev, Z. Grabarek, and J. Gergely Stabilization by a disulfide bond of the N-terminal domain of a mutant troponin C (TnC48/82) J. Biol. Chem. 266 1991 16622 16626
    • (1991) J. Biol. Chem. , vol.266 , pp. 16622-16626
    • Gusev, N.B.1    Grabarek, Z.2    Gergely, J.3
  • 33
    • 0019406008 scopus 로고
    • Effects of cations on affinity of calmodulin for calcium: Ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes
    • J. Haiech, C.B. Klee, and J.G. Demaille Effects of cations on affinity of calmodulin for calcium: ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes Biochemistry 20 1981 3890 3897
    • (1981) Biochemistry , vol.20 , pp. 3890-3897
    • Haiech, J.1    Klee, C.B.2    Demaille, J.G.3
  • 34
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • S. Linse, A. Helmersson, and S. Forsen Calcium binding to calmodulin and its globular domains J. Biol. Chem. 266 1991 8050 8054
    • (1991) J. Biol. Chem. , vol.266 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsen, S.3
  • 36
    • 0028927330 scopus 로고
    • 2+ binding to calmodulin - Proteolytic susceptibility of E31 and E87 indicates interdomain interactions
    • 2+ binding to calmodulin - proteolytic susceptibility of E31 and E87 indicates interdomain interactions Biochemistry 34 1995 1179 1196
    • (1995) Biochemistry , vol.34 , pp. 1179-1196
    • Pedigo, S.1    Shea, M.A.2
  • 37
    • 0033527588 scopus 로고    scopus 로고
    • Structural dynamics in the C-terminal domain of calmodulin at low calcium levels
    • A. Malmendal, J. Evenas, S. Forsen, and M. Akke Structural dynamics in the C-terminal domain of calmodulin at low calcium levels J. Mol. Biol. 293 1999 883 899
    • (1999) J. Mol. Biol. , vol.293 , pp. 883-899
    • Malmendal, A.1    Evenas, J.2    Forsen, S.3    Akke, M.4
  • 38
    • 0028980851 scopus 로고
    • Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner
    • M.X. Li, S.M. Gagne, S. Tsuda, C.M. Kay, L.B. Smillie, and B.D. Sykes Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner Biochemistry 34 1995 8330 8340
    • (1995) Biochemistry , vol.34 , pp. 8330-8340
    • Li, M.X.1    Gagne, S.M.2    Tsuda, S.3    Kay, C.M.4    Smillie, L.B.5    Sykes, B.D.6
  • 39
    • 0030612884 scopus 로고    scopus 로고
    • NMR studies of Ca2+ binding to the regulatory domains of cardiac and E41A skeletal muscle troponin C reveal the importance of site I to energetics of the induced structural changes
    • M.X. Li, S.M. Gagne, L. Spyracopoulos, C. Kloks, G. Audette, and M. Chandra NMR studies of Ca2+ binding to the regulatory domains of cardiac and E41A skeletal muscle troponin C reveal the importance of site I to energetics of the induced structural changes Biochemistry 36 1997 12519 12525
    • (1997) Biochemistry , vol.36 , pp. 12519-12525
    • Li, M.X.1    Gagne, S.M.2    Spyracopoulos, L.3    Kloks, C.4    Audette, G.5    Chandra, M.6
  • 42
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • O. Herzberg, and M.N. James Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution J. Mol. Biol. 203 1988 761 779
    • (1988) J. Mol. Biol. , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.2
  • 43
    • 0031576345 scopus 로고    scopus 로고
    • Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution
    • N.C. Strynadka, M. Cherney, A.R. Sielecki, M.X. Li, L.B. Smillie, and M.N. James Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution J. Mol. Biol. 273 1997 238 255
    • (1997) J. Mol. Biol. , vol.273 , pp. 238-255
    • Strynadka, N.C.1    Cherney, M.2    Sielecki, A.R.3    Li, M.X.4    Smillie, L.B.5    James, M.N.6
  • 45
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 48
    • 0031058188 scopus 로고    scopus 로고
    • Maximum likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength diffraction methods
    • E. de La Fortelle, and G. Bricogne Maximum likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 49
    • 84889120137 scopus 로고
    • Improved methods for building protein molecules in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein molecules in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 52
  • 53
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model data visualization using persistence of vision ray-tracing
    • T.D. Fenn, D. Ringe, and G.A. Petsko POVScript+: a program for model data visualization using persistence of vision ray-tracing J. Appl. Crystallog. 36 2003 944 947
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 54
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 56
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • W.E. Meador, A.R. Means, and F.A. Quiocho 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
  • 58
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brunger Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.