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Protein Science (2007), 16:1914-1926. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin)

Michael T. Henzl1 and John J. Tanner1,2

1 Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri 65211, USA
2 Department of Chemistry, University of Missouri-Columbia, Columbia, Missouri 65211, USA

(RECEIVED February 22, 2007; FINAL REVISION June 12, 2007; ACCEPTED June 13, 2007)

Relative to other parvalbumin isoforms, the mammalian beta-parvalbumin (oncomodulin) displays attenuated divalent ion affinity. High-resolution structural data for the Ca2+-bound protein have provided little insight into the physical basis for this behavior, prompting an examination of the unliganded state. This article describes the solution structure and peptide backbone dynamics of Ca2+-free rat beta-parvalbumin (beta-PV). Ca2+ removal evidently provokes significant structural alterations. Interaction between the D helix and the AB domain in the Ca2+-bound protein is greatly diminished in the apo-form, permitting the D helix to straighten. There is also a significant reorganization of the hydrophobic core and a concomitant remodeling of the interface between the AB and CD-EF domains. These modifications perturb the orientation of the C and D helices, and the energetic penalty associated with their reversal could contribute to the low-affinity signature of the CD site. By contrast, Ca2+ removal causes a comparatively minor perturbation of the E and F helices, consistent with the more typical divalent ion affinity observed for the EF site. Ca2+-free rat beta-PV retains structural rigidity on the picosecond–nanosecond timescale. At 20°C, the majority of amide vectors show no evidence for motion on timescales above 20 ps, and the average order parameter for the entire molecule is 0.92.

Keywords: calcium-binding protein; EF-hand protein; parvalbumin; oncomodulin; NMR; structure; dynamics


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M. T. Henzl and J. J. Tanner
Solution structure of Ca2+-free rat {alpha}-parvalbumin
Protein Sci., March 1, 2008; 17(3): 431 - 438.
[Abstract] [Full Text] [PDF]


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