1omr: Difference between revisions
New page: left|200px<br /><applet load="1omr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1omr, resolution 1.50Å" /> '''non-myristoylated wi... |
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[[Image:1omr.gif|left|200px]]<br /><applet load="1omr" size=" | [[Image:1omr.gif|left|200px]]<br /><applet load="1omr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1omr, resolution 1.50Å" /> | caption="1omr, resolution 1.50Å" /> | ||
'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3'''<br /> | '''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3'''<br /> | ||
==Overview== | ==Overview== | ||
Recoverin is a Ca2+-regulated signal transduction modulator found in | 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== | ||
1OMR 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:// | 1OMR 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=1OMR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Granzin, J.]] | [[Category: Granzin, J.]] | ||
[[Category: Weiergraber, O | [[Category: Weiergraber, O H.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
[[Category: helix-loop-helix]] | [[Category: helix-loop-helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:26 2008'' | ||
Revision as of 12:19, 21 February 2008
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non-myristoylated wild-type bovine recoverin 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
1OMR is a Single protein structure of sequence from Bos taurus with CA as ligand. 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
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