1omv: Difference between revisions

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New page: left|200px<br /><applet load="1omv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omv, resolution 1.90Å" /> '''non-myristoylated bo...
 
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[[Image:1omv.jpg|left|200px]]<br /><applet load="1omv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1omv.jpg|left|200px]]<br /><applet load="1omv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1omv, resolution 1.90&Aring;" />
caption="1omv, resolution 1.90&Aring;" />
'''non-myristoylated bovine recoverin (E85Q mutant) with calcium bound to EF-hand 3'''<br />
'''non-myristoylated bovine recoverin (E85Q mutant) with calcium bound to EF-hand 3'''<br />


==Overview==
==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.
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==
==About this Structure==
1OMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OMV OCA].  
1OMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMV OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Granzin, J.]]
[[Category: Granzin, J.]]
[[Category: Weiergraber, O.H.]]
[[Category: Weiergraber, O H.]]
[[Category: CA]]
[[Category: CA]]
[[Category: ef-hand]]
[[Category: ef-hand]]
[[Category: helix-loop-helix]]
[[Category: helix-loop-helix]]


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