The linker of des-Glu84-calmodulin is bent.
The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.
Raghunathan
S
S
Department of Biology, University of Virginia, Charlottesville 22901.
Chandross
R J
RJ
Cheng
B P
BP
Persechini
A
A
Sobottka
S E
SE
Kretsinger
R H
RH
D000595:Amino Acid Sequence; D002147:Calmodulin / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D002147:Calmodulin; C082348:des(Glu(84))-calmodulin