We present here the first evidence, obtained by the use of small-angle X-ray scattering, of the solution structures of chimeras constructed from yeast (Saccharomyces cerevisiae, Sc) and chicken (Gallus gallus, Gg) calmodulin (CaM). The chimeric proteins used in this study are Sc(1-129)/Gg(130-148), Sc(1-128)/Gg(129-148), Sc(1-87)/Gg(88-148), and Sc(1-72)/Gg(73-148) CaMs, in which Sc(1-)(n)() and Gg(()(n)(+1)-148) descend from yeast and chicken CaM in the chimeric proteins, respectively. Under the Ca(2+)-saturated condition, the solution structure of Sc(1-128)/Gg(129-148) CaM has a dumbbell-like shape which is characteristic of vertebrate-type CaM, while that of Sc(1-129)/Gg(130-148) CaM takes an intermediate structure between the dumbbell-like shape and a compact globular shape. The results provide the direct evidence that the replacement of Asp(129) with Ser(129) induces an interaction between two lobes of Sc(1-129)/Gg(130-148) CaM and brings them close together. It implies that a site interacting with the N-lobe is induced in the C-lobe, although site IV that is unable to bind Ca(2+) hinders the ability of the C-lobe to undergo the conformational change to the full open state. In the presence of both Ca(2+) and a peptide synthesized to mimic the CaM binding domain on myosin light chain kinase, MLCK-22p, the solution structures of these chimeric CaMs take a similar compact globular shape but their interactions are quite different. The solution structure and interactions of Sc(1-72)/Gg(73-148) CaM are similar to those of Sc(1-87)/Gg(88-148) CaM. The structure of Sc(1-87)/Gg(88-148) CaM is similar to that of Sc(1-128)/Gg(129-148) CaM, but their interactions are different. The result indicates that the replacement of Glu(119) with Ala(119) has a critical effect on their interactions. Thus, the functional differences among these chimeric CaMs, which have been reported previously [Nakashima, K., et al. (1996) Biochemistry 35, 5602-5610], have been interpreted on the basis of the structures and interactions.
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Evidence ID | Analyze ID | Gene/Complex | Systematic Name/Complex Accession | Qualifier | Gene Ontology Term ID | Gene Ontology Term | Aspect | Annotation Extension | Evidence | Method | Source | Assigned On | Reference |
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Evidence ID | Analyze ID | Gene | Gene Systematic Name | Phenotype | Experiment Type | Experiment Type Category | Mutant Information | Strain Background | Chemical | Details | Reference |
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Evidence ID | Analyze ID | Gene | Gene Systematic Name | Disease Ontology Term | Disease Ontology Term ID | Qualifier | Evidence | Method | Source | Assigned On | Reference |
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Evidence ID | Analyze ID | Regulator | Regulator Systematic Name | Target | Target Systematic Name | Direction | Regulation of | Happens During | Regulator Type | Direction | Regulation Of | Happens During | Method | Evidence | Strain Background | Reference |
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Site | Modification | Modifier | Source | Reference |
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Evidence ID | Analyze ID | Interactor | Interactor Systematic Name | Interactor | Interactor Systematic Name | Allele | Assay | Annotation | Action | Phenotype | SGA score | P-value | Source | Reference | Note |
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Complement ID | Locus ID | Gene | Species | Gene ID | Strain background | Direction | Details | Source | Reference |
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Evidence ID | Analyze ID | Dataset | Description | Keywords | Number of Conditions | Reference |
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