1omv
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Gene: | RCV1 (Bos taurus) | ||||||
| Related: | 1OMR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
non-myristoylated bovine recoverin (E85Q mutant) with calcium bound to EF-hand 3
Overview
Recoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.
About this Structure
1OMV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin., Weiergraber OH, Senin II, Philippov PP, Granzin J, Koch KW, J Biol Chem. 2003 Jun 20;278(25):22972-9. Epub 2003 Apr 9. PMID:12686556
Page seeded by OCA on Sun Mar 30 22:47:30 2008
