1cx4

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spinqualitylabelsall models 1cx4, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A DELETION MUTANT OF THE TYPE II BETA REGULATORY SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE

Overview

BACKGROUND: Cyclic AMP binding domains possess common structural features, yet are diversely coupled to different signaling modules. Each cAMP, binding domain receives and transmits a cAMP signal; however, the, signaling networks differ even within the same family of regulatory, proteins as evidenced by the long-standing biochemical and physiological, differences between type I and type II regulatory subunits of, cAMP-dependent protein kinase. RESULTS: We report the first type II, regulatory subunit crystal structure, which we determined to 2.45 A, resolution and refined to an R factor of 0.176 with a free R factor of, 0.198. This new structure of the type II beta regulatory subunit of, cAMP-dependent protein kinase demonstrates that the relative orientations, of the two tandem cAMP binding domains are very different in the type II, beta as compared to the type I alpha regulatory subunit. Each structural, unit for binding cAMP contains the highly conserved phosphate binding, cassette that can be considered the "signature" motif of cAMP binding, domains. This motif is coupled to nonconserved regions that link the cAMP, signal to diverse structural and functional modules. CONCLUSIONS: Both the, diversity and similarity of cAMP binding sites are demonstrated by this, new type II regulatory subunit structure. The structure represents an, intramolecular paradigm for the cooperative triad that links two cAMP, binding sites through a domain interface to the catalytic subunit of, cAMP-dependent protein kinase. The domain interface surface is created by, the binding of only one cAMP molecule and is enabled by amino acid, sequence variability within the peptide chain that tethers the two domains, together.

About this Structure

1CX4 is a Single protein structure of sequence from Rattus norvegicus with CMP as ligand. Full crystallographic information is available from OCA.

Reference

Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit., Diller TC, Madhusudan, Xuong NH, Taylor SS, Structure. 2001 Jan 10;9(1):73-82. PMID:11342137

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