1avj

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

CALMODULIN-TYPE TCH2 PROTEIN FROM ARABIDOPSIS, THEORETICAL MODEL

spinqualitylabelsall models 1avj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Plants adapt to various stresses by developmental alterations that render them less easily damaged. Expression of the TCH2 gene of Arabidopsis is strongly induced by stimuli such as touch and wind. The gene product, TCH2, belongs to the calmodulin (CaM) family of proteins and contains four highly conserved Ca(2+)-binding EF-hands. We describe here the structure of TCH2 in the fully Ca(2+)-saturated form, constructed using comparative molecular modeling, based on the x-ray structure of paramecium CaM. Like known CaMs, the overall structure consists of two globular domains separated by a linker helix. However, the linker region has added flexibility due to the presence of 5 glycines within a span of 6 residues. In addition, TCH2 is enriched in Lys and Arg residues relative to other CaMs, suggesting a preference for targets which are more negatively charged. Finally, a pair of Cys residues in the C-terminal domain, Cys126 and Cys131, are sufficiently close in space to form a disulfide bridge. These predictions serve to direct future biochemical and structural studies with the overall aim of understanding the role of TCH2 in the cellular response of Arabidopsis to environmental stimuli. Comparative modeling of the three-dimensional structure of the calmodulin-related TCH2 protein from Arabidopsis.,Khan AR, Johnson KA, Braam J, James MN Proteins. 1997 Jan;27(1):144-53. PMID:9037719 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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