1omr: Difference between revisions
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|PDB= 1omr |SIZE=350|CAPTION= <scene name='initialview01'>1omr</scene>, resolution 1.50Å | |PDB= 1omr |SIZE=350|CAPTION= <scene name='initialview01'>1omr</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1omv|1OMV]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omr OCA], [http://www.ebi.ac.uk/pdbsum/1omr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1omr RCSB]</span> | |||
}} | }} | ||
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[[Category: Granzin, J.]] | [[Category: Granzin, J.]] | ||
[[Category: Weiergraber, O H.]] | [[Category: Weiergraber, O H.]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
[[Category: helix-loop-helix]] | [[Category: helix-loop-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:26 2008'' | ||
Revision as of 22:47, 30 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | |||||||
| Gene: | RCV1 (Bos taurus) | ||||||
| Related: | 1OMV
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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