1omr: Difference between revisions
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[[Image:1omr.gif|left|200px]] | [[Image:1omr.gif|left|200px]] | ||
'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3''' | {{Structure | ||
|PDB= 1omr |SIZE=350|CAPTION= <scene name='initialview01'>1omr</scene>, resolution 1.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |||
}} | |||
'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OMR is a [ | 1OMR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12686556 12686556] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: helix-loop-helix]] | [[Category: helix-loop-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:57 2008'' | ||
Revision as of 14:12, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | |||||||
| Gene: | RCV1 (Bos taurus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3
OverviewOverview
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 StructureAbout this Structure
1OMR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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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