1OMR

non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3

Summary for 1OMR

• Entry DOI: 10.2210/pdb1omr/pdb
• Related: 1OMV
• Descriptor: recoverin, CALCIUM ION (3 entities in total)
• Functional Keywords: ef-hand, helix-loop-helix, metal binding protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 23275.29

Authors

Weiergraber, O.H.,Granzin, J. (deposition date: 2003-02-26, release date: 2003-11-25, Last modification date: 2023-10-25)

Primary citation

Weiergraber, O.H.,Senin, I.I.,Philippov, P.P.,Granzin, J.,Koch, K.-W.
Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin
J.Biol.Chem., 278:22972-22979, 2003

PubMed Abstract: 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.

PubMed: 12686556
DOI: 10.1074/jbc.M300447200

Experimental method

X-RAY DIFFRACTION (1.5 Å)