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| | ==Crystal structure of non-myristoylated recoverin with Cysteine-39 oxidized to sulfenic acid== | | ==Crystal structure of non-myristoylated recoverin with Cysteine-39 oxidized to sulfenic acid== |
| - | <StructureSection load='4m2q' size='340' side='right' caption='[[4m2q]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4m2q' size='340' side='right'caption='[[4m2q]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m2q]] 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=4M2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M2Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m2q]] 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=4M2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M2Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </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>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></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=4m2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2q OCA], [https://pdbe.org/4m2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m2q RCSB], [https://www.ebi.ac.uk/pdbsum/4m2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2q ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omr|1omr]], [[4m2o|4m2o]], [[4m2p|4m2p]], [[4mlw|4mlw]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCV1, RCVRN, Recoverin ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2q OCA], [http://pdbe.org/4m2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m2q RCSB], [http://www.ebi.ac.uk/pdbsum/4m2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2q 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Chakrabarti, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Kern, D]] | + | [[Category: Chakrabarti K]] |
| - | [[Category: Kumar, R Prem]] | + | [[Category: Kern D]] |
| - | [[Category: Oprian, D D]] | + | [[Category: Oprian DD]] |
| - | [[Category: Calcium binding protein]] | + | [[Category: Prem Kumar R]] |
| - | [[Category: Ef hand]]
| + | |
| - | [[Category: Inhibits rhodopsin kinase]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Retina]]
| + | |
| - | [[Category: Rhodopsin kinase]]
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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]
Publication Abstract from PubMed
Recoverin, a 23-kDa Ca(2+)-binding protein of the neuronal calcium sensing (NCS) family, inhibits rhodopsin kinase, a Ser/Thr kinase responsible for termination of photoactivated rhodopsin in rod photoreceptor cells. Recoverin has two functional EF hands and a myristoylated N terminus. The myristoyl chain imparts cooperativity to the Ca(2+)-binding sites through an allosteric mechanism involving a conformational equilibrium between R and T states of the protein. Ca(2+) binds preferentially to the R state; the myristoyl chain binds preferentially to the T state. In the absence of myristoylation, the R state predominates, and consequently, binding of Ca(2+) to the non-myristoylated protein is not cooperative. We show here that a mutation, C39A, of a highly conserved Cys residue among NCS proteins, increases the apparent cooperativity for binding of Ca(2+) to non-myristoylated recoverin. The binding data can be explained by an effect on the T/R equilibrium to favor the T state without affecting the intrinsic binding constants for the two Ca(2+) sites.
A Highly Conserved Cysteine of Neuronal Calcium-sensing Proteins Controls Cooperative Binding of Ca2+ to Recoverin.,Ranaghan MJ, Kumar RP, Chakrabarti KS, Buosi V, Kern D, Oprian DD J Biol Chem. 2013 Dec 13;288(50):36160-7. doi: 10.1074/jbc.M113.524355. Epub 2013, Nov 4. PMID:24189072[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
- ↑ Ranaghan MJ, Kumar RP, Chakrabarti KS, Buosi V, Kern D, Oprian DD. A Highly Conserved Cysteine of Neuronal Calcium-sensing Proteins Controls Cooperative Binding of Ca2+ to Recoverin. J Biol Chem. 2013 Dec 13;288(50):36160-7. doi: 10.1074/jbc.M113.524355. Epub 2013, Nov 4. PMID:24189072 doi:http://dx.doi.org/10.1074/jbc.M113.524355
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