Structural differences among subfamilies of EF-hand proteins-A view from the pseudo two-fold symmetry axis

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 11, 2014, Pages 2915-2924

  Kawasaki, Hiroshi ^a   Kretsinger, Robert H ^b  

^a YOKOHAMA CITY UNIVERSITY   (Japan)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Calcium; EF hand; EF lobe; Evolution; Function; Structural comparison; Symmetry

Indexed keywords

CALCIUM; CALCINEURIN; CALCIUM BINDING PROTEIN; CALMODULIN; MYOSIN LIGHT CHAIN; PROTEIN S 100; TROPONIN C;

ARTICLE; CONFORMATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TARGETING; CHEMISTRY; PROTEIN CONFORMATION;

CALCINEURIN; CALCIUM-BINDING PROTEINS; CALMODULIN; EF HAND MOTIFS; MYOSIN LIGHT CHAINS; PROTEIN CONFORMATION; S100 PROTEINS; TROPONIN C;

EID: 84934945008     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24562     Document Type: Article

References (40)

1. Kawasaki H, Nakayama S, Kretsinger RH. Classification and evolution of EF-hand proteins. Biometals 1998:11;277-295.
2. Clapham DE. Calcium signaling. Cell 2007:131;1047-1058.
3. Tufty RM, Kretsinger RH. Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 1975:187;167-169.
4. 1H NMR structural evidence. Science 1990:249;280-283.
5. Wójcik J, Góral J, Pawłowski K, Bierzyński A. Isolated calcium-binding loops of EF-hand proteins can dimerize to form a native-like structure†. Biochemistry (Mosc.) 1997:36;680-687.
6. Kawasaki H, Kretsinger RH. Analysis of the movements of helices in EF-hands. Proteins Struct Funct Bioinforma 2012:80;2592-2600.
7. Nakayama S, Kawasaki H, Kretsinger R. Calcium Homeost. In: Carafoli PDE, Krebs P-DDJ, editors. Berlin Heidelberg: Springer; 2000. pp 29-58.
8. Kawasaki H, Kretsinger RH. Calcium-binding proteins. 1: EF-hands. Protein Profile 1994:1;343-517.
9. Nakayama S, Moncrief ND, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J Mol Evol 1992:34;416-448.
10. Bhattacharya S, Bunick CG, Chazin WJ. Target selectivity in EF-hand calcium binding proteins. Biochim Biophys Acta BBA - Mol. Cell Res 2004:1742;69-79.
11. Vetter SW, Leclerc E. Novel aspects of calmodulin target recognition and activation. Eur J Biochem 2003:270;404-414.
12. Houdusse A, Cohen C. Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation. Struct Lond Engl 1993 1996:4;21-32.
13. Ohtsuki I. Regul. Mech. Striated Muscle Contract. In: Ebashi S, Ohtsuki I, editors. Japan: Springer, 2007. pp 21-36.
14. Donato R, Cannon BR, Sorci G, Riuzzi F, Hsu K, Weber DJ, Geczy CL. Functions of S100 proteins. Curr Mol Med 2013:13;24-57.
15. 2+ Buffers. Cold Spring Harb Perspect Biol 2010:2;a004051.
16. Rezvanpour A, Shaw GS. Unique S100 target protein interactions. Gen Physiol Biophys 2009:28Spec No Focus;F39-F46.
17. Olinger E, Schwaller B, Loffing J, Gailly P, Devuyst O. Parvalbumin: calcium and magnesium buffering in the distal nephron. Nephrol Dial Transplant 2012:27;3988-3994.
18. Yap KL, Ames JB, Swindells MB, Ikura M. Calcium-Bind. Protein Protoc. Vol. 2 Methods Tech. In: Vogel HJ, editor. New York: Springer, 2002:317-324.
19. Yap KL, Ames JB, Swindells MB, Ikura M. Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins Struct Funct Bioinforma 1999:37;499-507.
20. Babini E, Bertini I, Capozzi F, Luchinat C, Quattrone A, Turano M. Principal component analysis of the conformational freedom within the EF-Hand superfamily. J Proteome Res 2005:4;1961-1971.
21. Wang X, Mercier P, Letourneau P-J, Sykes BD. Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies. Protein Sci 2005:14;2447-2460.
22. Hoeflich KP, Ikura M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 2002:108;739-742.
23. Ames JB, Lim S. Molecular structure and target recognition of neuronal calcium sensor proteins. Biochim Biophys Acta 2012:1820;1205-1213.
24. Swain AL, Kretsinger RH, Amma EL. Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution. J Biol Chem 1989:264;16620-16628.
25. Permyakov EA, Medvedkin VN, Mitin YV, Kretsinger RH. Noncovalent complex between domain AB and domains CD*EF of parvalbumin. Biochim Biophys Acta BBA - Protein Struct Mol Enzymol 1991:1076;67-70.
26. Croall DE, Ersfeld K. The calpains: modular designs and functional diversity. Genome Biol 2007:8;218.
27. 2+-binding proteins. Biochim Biophys Acta BBA - Proteins Proteomics 2002:1600;51-60.
28. Head JF, Inouye S, Teranishi K, Shimomura O. The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature 2000:405;372-376.
29. 2+-loaded calbindin-D28K. Nat Struct Mol Biol 2006:13;641-647.
30. Vijay-Kumar S, Cook WJ. Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2·0 Å resolution. J Mol Biol 1992:224;413-426.
31. Théret I, Baladi S, Cox JA, Sakamoto H, Craescu CT. Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement†. Biochemistry (Mosc.) 2000:39;7920-7926.
32. Bourne Y, Taylor P, Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 1995:83;503-512.
33. Bourne Y, Taylor P, Radić Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003:22;1-12.
34. Tsigelny I, Shindyalov IN, Bourne PE, Südhof TC, Taylor P. Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations. Protein Sci 2000:9;180-185.
35. Hohenester E, Maurer P, Timpl R. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J 1997:16;3778-3786.
36. Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ. Structure of a WW domain containing fragment of dystrophin in complex with β-dystroglycan. Nat Struct Mol Biol 2000:7;634-638.
37. Essen L-O, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 1996:380;595-602.
38. Chen X, Vinkemeier U, Zhao Y, Jeruzalmi D, Darnell JE Jr, Kuriyan J. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 1998:93;827-839.
39. Becker S, Groner B, Müller CW. Three-dimensional structure of the Stat3β homodimer bound to DNA. Nature 1998:394;145-151.
40. Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 1999:398;84-90.