2r2i: Difference between revisions
New page: left|200px<br /><applet load="2r2i" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r2i, resolution 2.000Å" /> '''Myristoylated Guany... |
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==Overview== | ==Overview== | ||
Guanylate cyclase-activating proteins (GCAPs) are Ca(2+)-binding proteins | 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== | ==About this Structure== | ||
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[[Category: vision]] | [[Category: vision]] | ||
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Revision as of 16:44, 21 February 2008
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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 with CA, MYR and BME as ligands. 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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