4yi9: Difference between revisions
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<StructureSection load='4yi9' size='340' side='right'caption='[[4yi9]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='4yi9' size='340' side='right'caption='[[4yi9]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yi9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4yi9]] 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=4YI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YI9 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | </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=NA:SODIUM+ION'>NA</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=4yi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yi9 OCA], [https://pdbe.org/4yi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yi9 RCSB], [https://www.ebi.ac.uk/pdbsum/4yi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yi9 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Oprian DD]] | ||
[[Category: | [[Category: Prem Kumar R]] | ||
[[Category: Ranaghan | [[Category: Ranaghan MJ]] | ||
Revision as of 11:15, 3 May 2023
Crystal structure of non-myristoylated E153A recoverin at 1.35 A resolution with a sodium ion bound to EF-hand 2 and calcium ion bound to EF-hand 3Crystal structure of non-myristoylated E153A recoverin at 1.35 A resolution with a sodium ion bound to EF-hand 2 and 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 (Rv), a small Ca2+-binding protein that inhibits rhodopsin kinase (RK), has four EF hands, two of which are functional (EF2 and EF3). Activation requires Ca2+ in both EF hands, but crystal structures have never been observed with Ca2+ ions in both sites; all previous structures have Ca2+ bound only to EF3. We suspected that this was due to an intermolecular crystal contact between T80 and a surface glutamate (E153) that precluded coordination of a Ca2+ ion in EF2. We constructed the E153A mutant, determined its X-ray crystal structure to 1.2 A resolution, and show that 2 Ca2+ ions are bound, one in EF3 and one in EF2. Additionally, several other residues are shown to adopt conformations in the 2Ca2+-structure not seen previously and not seen in a second structure of the E153A mutant containing Na+ instead of Ca2+ in the EF2 site. The side-chain rearrangements in these residues form a 28 A long allosteric cascade along the surface of the protein connecting the Ca2+-binding site of EF2 with the active-site pocket responsible for binding RK. Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional EF-Hands.,Kumar RP, Ranaghan MJ, Ganjei AY, Oprian DD Biochemistry. 2015 Nov 19. PMID:26584024[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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