4mlw: Difference between revisions
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==Crystal structure of non-myristoylated recoverin at 1.45 A resolution with calcium bound to EF-hand 3== | ==Crystal structure of non-myristoylated recoverin at 1.45 A resolution with calcium bound to EF-hand 3== | ||
<StructureSection load='4mlw' size='340' side='right' caption='[[4mlw]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='4mlw' size='340' side='right' caption='[[4mlw]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omr|1omr]], [[4m2q|4m2q]], [[4m2o|4m2o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omr|1omr]], [[4m2q|4m2q]], [[4m2o|4m2o]]</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='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=4mlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mlw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mlw RCSB], [http://www.ebi.ac.uk/pdbsum/4mlw PDBsum]</span></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=4mlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mlw OCA], [http://pdbe.org/4mlw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mlw RCSB], [http://www.ebi.ac.uk/pdbsum/4mlw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mlw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4mlw" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 20:53, 4 August 2016
Crystal structure of non-myristoylated recoverin at 1.45 A resolution with calcium bound to EF-hand 3Crystal structure of non-myristoylated recoverin at 1.45 A resolution with calcium bound to EF-hand 3
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 PubMedRecoverin, 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 AlsoReferences
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