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| | <StructureSection load='1omv' size='340' side='right'caption='[[1omv]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1omv' size='340' side='right'caption='[[1omv]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1omv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OMV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1omv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1omr|1omr]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1omv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omv OCA], [https://pdbe.org/1omv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omv RCSB], [https://www.ebi.ac.uk/pdbsum/1omv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omv ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1omv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omv OCA], [http://pdbe.org/1omv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omv RCSB], [http://www.ebi.ac.uk/pdbsum/1omv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1omv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RECO_BOVIN RECO_BOVIN]] Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref> | + | [https://www.uniprot.org/uniprot/RECO_BOVIN RECO_BOVIN] Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Granzin, J]] | + | [[Category: Granzin J]] |
| - | [[Category: Weiergraber, O H]] | + | [[Category: Weiergraber OH]] |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Helix-loop-helix]]
| + | |
| - | [[Category: Metal binding protein]]
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| Structural highlights
Function
RECO_BOVIN Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hurley JB, Dizhoor AM, Ray S, Stryer L. Recoverin's role: conclusion withdrawn. Science. 1993 May 7;260(5109):740. PMID:8097896
- ↑ Kawamura S, Hisatomi O, Kayada S, Tokunaga F, Kuo CH. Recoverin has S-modulin activity in frog rods. J Biol Chem. 1993 Jul 15;268(20):14579-82. PMID:8392055
- ↑ Weiergraber OH, Senin II, Philippov PP, Granzin J, Koch KW. Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin. J Biol Chem. 2003 Jun 20;278(25):22972-9. Epub 2003 Apr 9. PMID:12686556 doi:10.1074/jbc.M300447200
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