Calcium-dependent stabilization of the central sequence between Met(76) and Ser(81) in vertebrate calmodulin

Biophysical Journal
Z Qin, Thomas C Squier

Abstract

Spin-label electron paramagnetic resonance (EPR) provides optimal resolution of dynamic and conformational heterogeneity on the nanosecond time-scale and was used to assess the structure of the sequence between Met(76) and Ser(81) in vertebrate calmodulin (CaM). Previous fluorescence resonance energy transfer and anisotropy measurements indicate that the opposing domains of CaM are structurally coupled and the interconnecting central sequence adopts conformationally distinct structures in the apo-form and following calcium activation. In contrast, NMR data suggest that the opposing domains of CaM undergo independent rotational dynamics and that the sequence between Met(76) and Ser(81) in the central sequence functions as a flexible linker that connects two structurally independent domains. However, these latter measurements also resolve weak internuclear interactions that suggest the formation of transient helical structures that are stable on the nanosecond time-scale within the sequence between Met(76) and Asp(80) in apo-CaM (H. Kuboniwa, N. Tjandra, S. Grzekiek, H. Ren, C. B. Klee, and A. Bax, 1995, Nat. Struct. Biol. 2:768-776). This reported conformational heterogeneity was resolved using site-directed mutagenesis and spin...Continue Reading

References

Nov 15, 1979·Analytical Biochemistry·P A LanzettaO A Candia
Dec 20, 1992·Journal of Molecular Biology·R ChattopadhyayaF A Quiocho
Jun 1, 1992·Cell Calcium·R H Kretsinger
Nov 5, 1988·Journal of Molecular Biology·Y S BabuW J Cook
May 5, 1986·Journal of Molecular Biology·F W Studier, B A Moffatt
May 2, 1985·Nature·Y S BabuW J Cook
Feb 20, 1985·Journal of Molecular Biology·T N Tsalkova, P L Privalov
Aug 5, 1980·Biochemistry·D C LaPorteD R Storm
Sep 1, 1995·Nature Structural Biology·H KuboniwaA Bax
Sep 1, 1995·Nature Structural Biology·B E FinnS Forsén
Jun 15, 1995·European Journal of Biochemistry·N TjandraA Bax
Jan 1, 1995·Annual Review of Biophysics and Biomolecular Structure·A Crivici, M Ikura
Jun 4, 1993·Biochimica Et Biophysica Acta·A PersechiniH G Lee
Mar 1, 1996·Chemical Research in Toxicology·A F HühmerC Schöneich
Mar 1, 1996·Protein Science : a Publication of the Protein Society·P MukherjeaK Beckingham
Mar 25, 1998·Biophysical Journal·J GaoT C Squier
Apr 17, 1998·Biophysical Journal·W WriggersK Schulten

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Citations

Jul 19, 2005·Journal of the American Society for Mass Spectrometry·Nadezhda A GalevaThomas C Squier
Jan 8, 2008·Proceedings of the National Academy of Sciences of the United States of America·Hye Yoon ParkLois Pollack
Jun 5, 2014·Protein Science : a Publication of the Protein Society·Eric M JonesThomas G Spiro
Sep 16, 2009·Biophysical Journal·Valentina BorsiGiacomo Parigi
Dec 6, 2014·Biochemical and Biophysical Research Communications·Megan R McCarthyDavid D Thomas
Apr 11, 2014·The Protein Journal·Paula B Bowman, David Puett
Feb 13, 2020·Biophysical Journal·Megan R McCarthyDavid D Thomas
Sep 11, 2021·Frontiers in Molecular Biosciences·Jules NdeMargaret S Cheung

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