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Abstract:

EF-hands are Ca2+ binding motifs that are widely distributed throughout the entire living organism kingdom. At present, relatively little is known at a quantum mechanical level about the mechanisms that allow Ca 2+ to be recognized specifically by EF-hands and to induce a conformational switch from a compact ("closed") conformation to an "open" state that exposes a large patch of hydrophobic residues. Here, we present a study of NMR 15N chemical shifts based on ab initio quantum mechanical calculations carried out on a minimalist model system linking both Ca2+ binding sites across the β-sheet of an EF-hand domain. Calculated and experimentally determined chemical shift changes are correlated with structural changes induced upon metal binding. The effect of Ca2+ binding on these 15N shifts can be dissected into two main contributions: one from π-polarization of β-sheet amide groups and the other from rotation of an isoleucine side chain. By correlating this description with experimental evidence, different polarization states for the β-sheet amide groups were identified and linked to the overall conformation of different EF-hand domains. When all four β-sheet amide groups are polarized, the ab initio calculations in our model indicate a cooperative stabilization effect due to the establishment of a circular network of donor-acceptor interactions connecting the two Ca2+ ions across the β-sheet. The emerging hypothesis from our analysis is that this cooperative network of interactions is essential for stabilizing the "open" conformation of an EF-hand domain.

Registro:

Documento: Artículo
Título:Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins
Autor:Biekofsky, R.R.; Turjanski, A.G.; Estrin, D.A.; Feeney, J.; Pastore, A.
Filiación:Molecular Structure Division, Natl. Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom
Depto. Quim. Inorg./Anal./Quim.-Fis., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Calcium; Conformations; Hydrophobicity; Molecular structure; Nuclear magnetic resonance spectroscopy; Proteins; Binding motifs; Chemical shift; Metal binding; Biochemical engineering; amide; calcium ion; EF hand protein; isoleucine; protein; unclassified drug; ab initio calculation; article; beta sheet; binding site; calcium binding; calcium binding motif; conformational transition; ef hand domain; hydrogen bond; hydrophobicity; metal binding; nitrogen nuclear magnetic resonance; pi polarization; polarization; priority journal; protein conformation; protein domain; protein interaction; protein motif; quantum mechanics; Amino Acid Motifs; Amino Acid Sequence; Calcium; Calmodulin; Holoenzymes; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Nitrogen Isotopes; Protein Conformation; Protein Structure, Tertiary
Año:2004
Volumen:43
Número:21
Página de inicio:6554
Página de fin:6564
DOI: http://dx.doi.org/10.1021/bi0497852
Título revista:Biochemistry
Título revista abreviado:Biochemistry
ISSN:00062960
CODEN:BICHA
CAS:amide, 17655-31-1; calcium ion, 14127-61-8; isoleucine, 7004-09-3, 73-32-5; protein, 67254-75-5; Calcium, 7440-70-2; Calmodulin; Holoenzymes; Nitrogen Isotopes
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v43_n21_p6554_Biekofsky

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Citas:

---------- APA ----------
Biekofsky, R.R., Turjanski, A.G., Estrin, D.A., Feeney, J. & Pastore, A. (2004) . Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins. Biochemistry, 43(21), 6554-6564.
http://dx.doi.org/10.1021/bi0497852
---------- CHICAGO ----------
Biekofsky, R.R., Turjanski, A.G., Estrin, D.A., Feeney, J., Pastore, A. "Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins" . Biochemistry 43, no. 21 (2004) : 6554-6564.
http://dx.doi.org/10.1021/bi0497852
---------- MLA ----------
Biekofsky, R.R., Turjanski, A.G., Estrin, D.A., Feeney, J., Pastore, A. "Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins" . Biochemistry, vol. 43, no. 21, 2004, pp. 6554-6564.
http://dx.doi.org/10.1021/bi0497852
---------- VANCOUVER ----------
Biekofsky, R.R., Turjanski, A.G., Estrin, D.A., Feeney, J., Pastore, A. Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins. Biochemistry. 2004;43(21):6554-6564.
http://dx.doi.org/10.1021/bi0497852