2r2i

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(New page: 200px<br /><applet load="2r2i" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r2i, resolution 2.000&Aring;" /> '''Myristoylated Guany...)
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==Overview==
==Overview==
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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.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:13:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:44:10 2008''

Revision as of 16:44, 21 February 2008


2r2i, resolution 2.000Å

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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 , and 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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