2r2i | pdb_00002r2i
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| 2r2i, resolution 2.000Å | |||||||||||||
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| Ligands: | BME, CA, MYR | ||||||||||||
| Gene: | GUCA1A, GCAP1 (Gallus gallus) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Myristoylated Guanylate Cyclase Activating Protein-1 with Calcium Bound
Overview
Guanylate cyclase-activating proteins (GCAPs) are Ca(2+)-binding proteins myristoylated at the N terminus that regulate guanylate cyclases in photoreceptor cells and belong to the family of neuronal calcium sensors (NCS). Many NCS proteins display a recoverin-like "calcium-myristoyl switch" whereby the myristoyl group, buried inside the protein in the Ca(2+)-free state, becomes fully exposed upon Ca(2+) binding. Here we present a 2.0 A resolution crystal structure of myristoylated GCAP1 with Ca(2+) bound. The acyl group is buried inside Ca(2+)-bound GCAP1. This is in sharp contrast to Ca(2+)-bound recoverin, where the myristoyl group is solvent exposed. Furthermore, we provide direct evidence that the acyl group in GCAP1 remains buried in the Ca(2+)-free state and does not undergo switching. A pronounced kink in the C-terminal helix and the presence of the myristoyl group allow clustering of sequence elements crucial for GCAP1 activity.
About this Structure
2R2I is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Stabilizing function for myristoyl group revealed by the crystal structure of a neuronal calcium sensor, guanylate cyclase-activating protein 1., Stephen R, Bereta G, Golczak M, Palczewski K, Sousa MC, Structure. 2007 Nov;15(11):1392-402. PMID:17997965
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