4m2p: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4m2p]] 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=4M2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M2P FirstGlance]. <br> | <table><tr><td colspan='2'>[[4m2p]] 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=4M2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M2P 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]] 1.45Å</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=4m2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2p OCA], [https://pdbe.org/4m2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m2p RCSB], [https://www.ebi.ac.uk/pdbsum/4m2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2p 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=4m2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2p OCA], [https://pdbe.org/4m2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m2p RCSB], [https://www.ebi.ac.uk/pdbsum/4m2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 19:31, 20 September 2023
Crystal structure of a non-myristoylated C39D recoverin mutant with one calcium ion bound to EF-hand 3Crystal structure of a non-myristoylated C39D recoverin mutant with one calcium ion bound to EF-hand 3
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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