4m2q: Difference between revisions
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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 [ | <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=' | </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=' | <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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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 4m2q" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chakrabarti K]] | ||
[[Category: | [[Category: Kern D]] | ||
[[Category: Oprian | [[Category: Oprian DD]] | ||
[[Category: | [[Category: Prem Kumar R]] | ||
Latest revision as of 19:31, 20 September 2023
Crystal structure of non-myristoylated recoverin with Cysteine-39 oxidized to sulfenic acidCrystal structure of non-myristoylated recoverin with Cysteine-39 oxidized to sulfenic acid
Structural highlights
FunctionRECO_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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