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Structure of calmodulin refined at 2.2 A resolution.

Babu YS, Bugg CE, Cook WJ
J Mol Biol 204 191-204 (1988)
Cited: 597 times
EuropePMC logo PMID: 3145979

Abstract

The crystal structure of mammalian calmodulin has been refined at 2.2 A (1 A = 0.1 nm) resolution using a restrained least-squares method. The final crystallographic R-factor, based on 6685 reflections in the range 2.2 A less than or equal to d less than or equal to 5.0 A with intensities exceeding 2.5 sigma, is 0.175. Bond lengths and bond angles in the molecule have root-mean-square deviations from ideal values of 0.016 A and 1.7 degrees, respectively. The refined model includes residues 5 to 147, four Ca2+ and 69 water molecules per molecule of calmodulin. The electron density for residues 1 to 4 and 148 is poorly defined, and they are not included in the model. The molecule is shaped somewhat like a dumbbell, with an overall length of 65 A; the two lobes are connected by a seven-turn alpha-helix. Prominent secondary structural features include seven alpha-helices, four Ca2+-binding loops, and two short, double-stranded antiparallel beta-sheets between pairs of adjacent Ca2+-binding loops. The four Ca2+-binding domains in calmodulin have a typical EF hand conformation (helix-loop-helix) and are similar to those described in other Ca2+-binding proteins. The X-ray structure determination of calmodulin shows a large hydrophobic cleft in each half of the molecule. These hydrophobic regions probably represent the sites of interaction with many of the pharmacological agents known to bind to calmodulin.

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  1. Three-Dimensional Structure of Calmodulin. Babu YS, Sack JS, Greenhough TJ, Bugg CE, Means AR, Cook WJ Nature 315 37- (1985)
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  4. Crystallization and Preliminary X-Ray Investigation of Calmodulin. Cook WJ, Dedman JR, Means AR, Bugg CE J. Biol. Chem. 255 8152- (1980)

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