The structure of a calmodulin mutant with a deletion in the central helix: Implications for molecular recognition and protein binding

Structure

Volumn 5, Issue 5, 1997, Pages 613-622

  Tabernero, Lydia ^a,d   Taylor, Denise A ^b,e   Chandross, Ronald J ^c,f   VanBerkum, Mark F A ^b,g   Means, Anthony R ^b,h   Quiocho, Florante A ^b   Sack, John S ^a  

^a BRISTOL MYERS SQUIBB   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c University of Virginia ^*  (United States)

^d PURDUE UNIVERSITY   (United States)

^e Texas Medical Foundation   (United States)

^f Ctr of Advanced Res in Biotechnol   (United States)

^g WAYNE STATE UNIVERSITY   (United States)

^h DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

calcium; calmodulin; X ray structure

Indexed keywords

EID: 0031570287     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00217-7     Document Type: Article

References (38)

1. Ikura, M., Clore, G.M., Gronenborn, M., Zhu, G., Klee, C.B. & Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
2. Meador, W.E., Means, A.R. & Quiocho, F.A. (1992). Target enzyme recognition by calmodulin: 2.4Å structure of a calmodulin-peptide complex. Science 257, 1251-1255.
3. Meador, W.E., Means, A.R. & Quiocho, F.A. (1993). Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721.
4. Meador, W.E., George, S.E., Means, A.R. & Quiocho, F.A. (1995). X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants. Nat. Struct. Biol. 2, 943-945.
5. Kataoka, M., Head, J.F., Persechini, A., Kretsinger, R.H. & Engelman, D.M. (1991). Small angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominately α-helical conformation. Biochemistry 30, 1188-1192.
6. Putkey, J.A., Ono, T., VanBerkum, M.F.A. & Means, A.R. (1988). Functional significance of the central helix in calmodulin. J. Biol. Chem. 263, 11242-11249.
7. Craig, T.A., Watterson, D.M., Prendergast, F.G., Haiech, J. & Roberts, D.M. (1987). Site-specific mutagenesis of the α-helices of calmodulin. Effects of altering a charge cluster in the helix that links the two halves of calmodulin. J. Biol. Chem. 262, 3278-3284.
8. Weber, P.C., et al., & Watterson, D.M. (1989). Computational and site-specific mutagenesis analysis of the asymmetric charge distribution on calmodulin. Proteins 6, 70-85.
9. Tanaka, T. & Hidaka, H. (1980). Hydrophobic regions function in calmodulin enzyme interactions. J. Biol. Chem. 255, 11078-11080.
10. LaPorte, D.C., Wierman, B.M. & Storm, D.R. (1980). Calcium-induced exposure of a hydrophobic surface on calmodulin. Biochemistry 19, 3814-3819.
11. Babu, Y.S., Sack, J.S., Greenhough, T.J., Bugg, C.E., Means, A.R. & Cook, W.J. (1985). Three-dimensional structure of calmodulin. Nature 315, 37-40.
12. 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.
13. Chattopadhyaya, R., Meador, W.E., Means, A.R. & Quiocho, F.A. (1992). Calmodulin structure refined at 1.7 Å resolution. J. Mol. Biol. 228, 1177-1192.
14. Taylor, D.A., Sack, J.S., Maune, J.F., Beckingham, K. & Quiocho, F.A. (1991). Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2 Å resolution. J. Biol. Chem. 266, 21375-21380.
15. Ban, C., Ramakrishnan, B., Ling, K., Kung, C. & Sundaralingam, M. (1994). Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 Å resolution. Acta Cryst. D50, 50-63.
16. Rao, S.T., Wu, S., Satyshur, K.A., Ling, K.-Y., Kung, C. & Sundaralingam, M. (1993). Structure of Paramecium tetraurelia calmodulin at 1.8 Å resolution. Protein Sci. 2, 436-447.
17. 13C resonance assignment of calmodulin in solution by heterodimer multi-dimensional NMR spectroscopy. Biochemistry 30, 9216-9228.
18. Heidorn, D.B. & Trewhella, J. (1988). Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry 27, 909-915.
19. Raghunathan, S., Chandross, R.J., Cheng, B.-P., Persechini, A., Sobottka, S.E. & Kretsinger, R.H. (1993). The linker of des-Glu84-calmodulin is bent. Proc. Natl. Acad. Sci. USA 90, 6869-6873.
20. VanBerkum, M.F.A., George, S.E. & Means, A.R. (1990). Calmodulin activation of target enzymes. J. Biol. Chem. 265, 3750-3756.
21. Cox, J.A., Comte, M., Fitton, J.E. & DeGrado, W.F. (1985). The interaction of calmodulin with amphiphilic peptides. J. Biol. Chem. 260, 2527-2534.
22. O'Neil, K.T. & DeGrado, W.F. (1990). How calmodulin binds its targets: sequence independent recognition of amphiphilic α helices. Trends Biochem. Sci. 15, 59-64.
23. Charbonneau, H., et al., & Walsh, K.A. (1991). Evidence for domain organization within the 61 kDa calmodulin dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry 30, 7931-7940.
24. 2+/calmodulin-dependent protein kinase II. J. Biol. Chem. 264, 10884-10887.
25. Persechini, A., Blumenthal, D.K., Jarrett, H.W., Klee, C.B., Hardy, D.O. & Kretsinger, R.H. (1989). The effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding. J. Biol. Chem. 264, 8052-8058.
26. Presta, L.G. & Rose, G.D. (1988). Helix signals in proteins. Science 240, 1632-1641.
27. Aurora, R., Srinivasan, R. & Rose, G.D. (1994). Rules for α-helix termination by glycine. Science 264, 1126-1130.
28. Reeke, G.N. (1984). The ROCKS system of computer programs for macromolecular crystallography. J. Appl. Cryst. 17, 125-130.
29. Fitzgerald, P.M.D. (1988). MERLOT, an integrated package of computer programs for determination of crystal structures by molecular replacement. J. Appl. Cryst. 21, 273-278.
30. Brünger, A.T. (1992). X-PLOR Manual, Version 3.1. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT, USA.
31. Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
32. Lamzin V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
33. Hendrickson, W.A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
34. Sack, J.S. (1988). CHAIN - a crystallographic modeling program. J. Mol. Graph. 6, 224-225.
35. Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank. A computer based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
36. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
37. Smith, T.J. (1995). MolView: a program for analyzing and displaying atomic structures on the Macintosh personal computer. J. Mol. Graph. 13, 122-125.
38. Srinivan, R., Greeta, V. & Seetharaman, J. (1991). A unique or essentially unique parametric characterization of biopolymeric structures. J. Mol. Struct. Dyn. 8, a208.