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Volumn 270, Issue 11, 2003, Pages 2505-2512

NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea

Author keywords

Calcium binding; Calerythrin; NMR; Structure

Indexed keywords

CALCIUM BINDING PROTEIN; CALERYTHRIN; UNCLASSIFIED DRUG;

EID: 0038392574     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03623.x     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein
    • Kretsinger, R.H. & Nockolds, C.E. (1973) Carp muscle calcium-binding protein. J. Biol. Chem. 248, 3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 2
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T. & Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2, 758-767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 4
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu, Y.S., Bugg, C.E. & Cook, W.J. (1988) Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204, 191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 5
    • 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. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 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
  • 6
    • 0023643270 scopus 로고
    • A bacterial calcium-binding protein homologous to calmodulin
    • Swan, D.G., Hale, R.S., Dhillon, N. & Leadlay, P.F. (1987) A bacterial calcium-binding protein homologous to calmodulin. Nature 329, 84-85.
    • (1987) Nature , vol.329 , pp. 84-85
    • Swan, D.G.1    Hale, R.S.2    Dhillon, N.3    Leadlay, P.F.4
  • 7
    • 0024283992 scopus 로고
    • Sequence similarities in calcium-binding proteins
    • Cox, J.A. & Bairoch, A. (1988) Sequence similarities in calcium-binding proteins. Nature 331, 491.
    • (1988) Nature , vol.331 , pp. 491
    • Cox, J.A.1    Bairoch, A.2
  • 8
    • 0026517218 scopus 로고
    • Prokaryotic calcium-binding protein of the cal-modulin superfamily. Calcium binding to a Saccharopolyspora erythraea 20 kDa protein
    • Bylsma, N., Drakenberg, T., Andersson, I., Leadlay, P.F. & Forsén, S. (1992) Prokaryotic calcium-binding protein of the cal-modulin superfamily. Calcium binding to a Saccharopolyspora erythraea 20 kDa protein. FEBS Lett. 299, 44-47.
    • (1992) FEBS Lett. , vol.299 , pp. 44-47
    • Bylsma, N.1    Drakenberg, T.2    Andersson, I.3    Leadlay, P.F.4    Forsén, S.5
  • 9
    • 0033452878 scopus 로고    scopus 로고
    • NMR assignments, secondary structure, and global fold of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea
    • Aitio, H., Annila, A., Heikkinen, S., Thulin, E., Drakenberg, T. & Kilpeläinen, I. (1999) NMR assignments, secondary structure, and global fold of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea. Protein Sci. 8, 2580-2588.
    • (1999) Protein Sci. , vol.8 , pp. 2580-2588
    • Aitio, H.1    Annila, A.2    Heikkinen, S.3    Thulin, E.4    Drakenberg, T.5    Kilpeläinen, I.6
  • 10
    • 0029023503 scopus 로고
    • Sarcoplasmic calcium-binding protein
    • Hermann, A. & Cox, J.A. (1995) Sarcoplasmic calcium-binding protein. Comp. Biochem. Physiol. 111B, 337-345.
    • (1995) Comp. Biochem. Physiol. , vol.111 B , pp. 337-345
    • Hermann, A.1    Cox, J.A.2
  • 11
    • 0035933827 scopus 로고    scopus 로고
    • Calexcitin B is a new member of the sarcoplasmic calcium-binding protein family
    • Gombost, Z., Jeromin, A., Mal, T.K., Chakrabartty, A. & Ikura, M. (2001) Calexcitin B is a new member of the sarcoplasmic calcium-binding protein family. J. Biol. Chem. 276, 22529-22536.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22529-22536
    • Gombost, Z.1    Jeromin, A.2    Mal, T.K.3    Chakrabartty, A.4    Ikura, M.5
  • 12
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura, M. (1996) Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 14
    • 0034257019 scopus 로고    scopus 로고
    • Ion-induced conformational and stability changes in Nereis sarcoplasmic calcium binding protein: Evidence that the APO state is a molten globule
    • Christova, P., Cox, J.A. & Craescu, C.T. (2000) Ion-induced conformational and stability changes in Nereis sarcoplasmic calcium binding protein: Evidence that the APO state is a molten globule. Proteins 40, 177-184.
    • (2000) Proteins , vol.40 , pp. 177-184
    • Christova, P.1    Cox, J.A.2    Craescu, C.T.3
  • 16
    • 0035229806 scopus 로고    scopus 로고
    • A calcium-binding protein with four EF-hand motifs in Streptomyces ambofaciens
    • Yonekawa, T., Ohnishi, Y. & Horinouchi, S. (2001) A calcium-binding protein with four EF-hand motifs in Streptomyces ambofaciens. Biosci., Biotechnol., Biochem. 65, 156-160.
    • (2001) Biosci., Biotechnol., Biochem. , vol.65 , pp. 156-160
    • Yonekawa, T.1    Ohnishi, Y.2    Horinouchi, S.3
  • 17
    • 0024593454 scopus 로고
    • Calcium ion regulates aerial mycelium formation in actinomycetes
    • Natsume, M., Yasui, K. & Marumo, S. (1989) Calcium ion regulates aerial mycelium formation in actinomycetes. J. Antibiot. 42, 440-447.
    • (1989) J. Antibiot. , vol.42 , pp. 440-447
    • Natsume, M.1    Yasui, K.2    Marumo, S.3
  • 18
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • Hansen, M.R., Mueller, L. & Pardi, A. (1998) Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nature 5, 1065-1074.
    • (1998) Nature , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 19
  • 20
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, CA, USA
    • Goddard, T.D. & Kneller, D.G. SPARKY 3. University of California, San Francisco, CA, USA.
    • SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 21
    • 0000302902 scopus 로고    scopus 로고
    • An α/β-HSQC-α/β experiment for spin-state selective editing of IS cross peaks
    • Anderson, P., Annila, A. & Otting, G. (1998) An α/β-HSQC-α/β experiment for spin-state selective editing of IS cross peaks. J. Magn. Reson. 133, 364-367.
    • (1998) J. Magn. Reson. , vol.133 , pp. 364-367
    • Anderson, P.1    Annila, A.2    Otting, G.3
  • 22
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments
    • Weigelt, J. (1998) Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments. J. Am. Chem. Soc. 120, 10778-10779.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10778-10779
    • Weigelt, J.1
  • 23
    • 0034295408 scopus 로고    scopus 로고
    • Determination of backbone angle ψ in proteins using a TROSY-based α/β-HN (CO) CA-J experiment
    • Permi, P., Kilpeläinen, I. & Annila, A. (2000) Determination of backbone angle ψ in proteins using a TROSY-based α/β-HN (CO) CA-J experiment. J. Magn. Reson. 146, 255-259.
    • (2000) J. Magn. Reson. , vol.146 , pp. 255-259
    • Permi, P.1    Kilpeläinen, I.2    Annila, A.3
  • 24
    • 0034003170 scopus 로고    scopus 로고
    • Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings
    • Permi, P. & Annila, A. (2000) Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings. J. Biomol. NMR 16, 221.
    • (2000) J. Biomol. NMR , vol.16 , pp. 221
    • Permi, P.1    Annila, A.2
  • 27
    • 0032113480 scopus 로고    scopus 로고
    • A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information
    • Clore, G.M., Gronenborn, A.M. & Bax, A. (1998) A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133, 216-221.
    • (1998) J. Magn. Reson. , vol.133 , pp. 216-221
    • Clore, G.M.1    Gronenborn, A.M.2    Bax, A.3
  • 28
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 31
    • 0033577269 scopus 로고    scopus 로고
    • Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration
    • Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1999) Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration. J. Am. Chem. Soc. 121, 2337-2338.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2337-2338
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 32
    • 0003456102 scopus 로고
    • Yale University Press, New Haven, CT, USA
    • Brünger, A.T. (1992) XPLOR, Version 3.1. Yale University Press, New Haven, CT, USA.
    • (1992) XPLOR, Version 3.1
    • Brünger, A.T.1
  • 33
    • 0032012610 scopus 로고    scopus 로고
    • Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude
    • Clore, G.M., Gronenborn, A.M. & Tjandra, N. (1998) Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J. Magn. Reson. 131, 159-162.
    • (1998) J. Magn. Reson. , vol.131 , pp. 159-162
    • Clore, G.M.1    Gronenborn, A.M.2    Tjandra, N.3
  • 34
    • 0027383637 scopus 로고
    • 1H NMR
    • 1H NMR. Proteins 17, 297-309.
    • (1993) Proteins , vol.17 , pp. 297-309
    • Nilges, M.1
  • 35
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 36
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez, R., Chinea, G., Lopez, N., Pons, T. & Vriend, G. (1998) Homology modeling, model and software evaluation: three related resources. CABIOS 14, 523-528.
    • (1998) CABIOS , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 37
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macomolecular strucures
    • Koradi, R., Billeter, M. & Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macomolecular strucures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 38
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N.C. & James, M.N. (1989) Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58, 951-998.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 39
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 40
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • Toshiyuki, T., Ames, J.B., Harvey, T., Stryer, L. & Ikura, M. (1995) Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376, 444-447.
    • (1995) Nature , vol.376 , pp. 444-447
    • Toshiyuki, T.1    Ames, J.B.2    Harvey, T.3    Stryer, L.4    Ikura, M.5
  • 41
    • 0032841148 scopus 로고    scopus 로고
    • Recognition of protein folds via dipolar couplings
    • Annila, A., Aitio, H., Thulin, E. & Drakenberg, T. (1999) Recognition of protein folds via dipolar couplings. J. Biomol. NMR 14, 223-230.
    • (1999) J. Biomol. NMR , vol.14 , pp. 223-230
    • Annila, A.1    Aitio, H.2    Thulin, E.3    Drakenberg, T.4
  • 42
    • 0026545366 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution
    • Vijay-Kumar, S. & Cook, W.J. (1992) Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution. J. Mol. Biol. 224, 413-426.
    • (1992) J. Mol. Biol. , vol.224 , pp. 413-426
    • Vijay-Kumar, S.1    Cook, W.J.2
  • 43
    • 0027463062 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution
    • Cook, W.J., Jeffrey, L.C., Cox, J.A. & Vijay-Kumar, S. (1993) Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J. Mol. Biol. 229, 461-471.
    • (1993) J. Mol. Biol. , vol.229 , pp. 461-471
    • Cook, W.J.1    Jeffrey, L.C.2    Cox, J.A.3    Vijay-Kumar, S.4
  • 45
    • 0034718548 scopus 로고    scopus 로고
    • Symbiosis-specific expression of Rhizobium etli casA encoding a secreted calmodulin-related protein
    • Xi, C., Schoeters, E., Vanderleyden, J. & Michiels, J. (2000) Symbiosis-specific expression of Rhizobium etli casA encoding a secreted calmodulin-related protein. Proc. Natl Acad. Sci. USA 97, 11114-11119.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11114-11119
    • Xi, C.1    Schoeters, E.2    Vanderleyden, J.3    Michiels, J.4
  • 47
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • Vyas, N.K., Vyas, M.N. & Quiocho, F.A. (1987) A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature 327, 635-638.
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.