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| | <StructureSection load='2het' size='340' side='right'caption='[[2het]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='2het' size='340' side='right'caption='[[2het]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2het]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HET FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2het]] is a 4 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=2HET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HET 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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCV1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2het FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2het OCA], [https://pdbe.org/2het PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2het RCSB], [https://www.ebi.ac.uk/pdbsum/2het PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2het ProSAT]</span></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=2het FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2het OCA], [https://pdbe.org/2het PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2het RCSB], [https://www.ebi.ac.uk/pdbsum/2het PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2het ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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: Calcium binding]]
| + | |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Helix-loop-helix]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Recoverin]]
| + | |
| 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 Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
Tuning of a neuronal calcium sensor.,Weiergraber OH, Senin II, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:17015448[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, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW. Tuning of a neuronal calcium sensor. J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:17015448 doi:10.1074/jbc.M603700200
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