3uom: Difference between revisions

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<StructureSection load='3uom' size='340' side='right'caption='[[3uom]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
<StructureSection load='3uom' size='340' side='right'caption='[[3uom]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3uom]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UOM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3uom]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UOM 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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 2.02&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3us3|3us3]]</div></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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=3uom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uom OCA], [https://pdbe.org/3uom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uom RCSB], [https://www.ebi.ac.uk/pdbsum/3uom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uom 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=3uom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uom OCA], [https://pdbe.org/3uom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uom RCSB], [https://www.ebi.ac.uk/pdbsum/3uom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uom ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CASQ1_HUMAN CASQ1_HUMAN]] Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.<ref>PMID:22337878</ref> <ref>PMID:22337878</ref> 
[https://www.uniprot.org/uniprot/CASQ1_HUMAN CASQ1_HUMAN] Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.<ref>PMID:22337878</ref> <ref>PMID:22337878</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calsequestrin, the major calcium-storage protein of both cardiac and skeletal muscle, binds large amounts of Ca2+ in the sarcoplasmic reticulum and releases them during muscle contraction. For the first time, crystal structures of Ca2+-complexes for both human (hCASQ1) and rabbit skeletal calsequestrin (rCASQ1) were determined, clearly defining its Ca2+-sequestration capabilities through resolution of high- and low-affinity Ca2+-binding sites. rCASQ1 crystallized in low CaCl2 buffer revealed three high-affinity Ca2+ sites with trigonal bipyramidal, octahedral, and pentagonal bipyramidal coordination geometries, along with three low-affinity Ca2+ sites. hCASQ1 crystallized in high CaCl2 showed fifteen Ca2+ ions, which included the six Ca2+ ions in rCASQ1. Most of the low-affinity sites, some of which were mu-carboxylate-bridged, were established by the rotation of dimeric interfaces, indicating cooperative Ca2+-binding that is consistent with our atomic absorption spectroscopic data. Based on these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca2+-binding activity of calsequestrin.
 
High-capacity Ca2+-binding of human skeletal calsequestrin.,Sanchez EJ, Lewis KM, Danna BR, Kang C J Biol Chem. 2012 Feb 15. PMID:22337878<ref>PMID:22337878</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3uom" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Danna, B R]]
[[Category: Danna BR]]
[[Category: Kang, C H]]
[[Category: Kang CH]]
[[Category: Lewis, K M]]
[[Category: Lewis KM]]
[[Category: Nissen, M S]]
[[Category: Nissen MS]]
[[Category: Sanchez, E J]]
[[Category: Sanchez EJ]]
[[Category: Calcium binding]]
[[Category: Calcium-binding protein]]
[[Category: Sarcoplasmic reticulum]]
[[Category: Thioredoxin-like fold]]

Latest revision as of 14:04, 14 March 2024

Ca2+ complex of Human skeletal calsequestrin

3uom, resolution 2.02Å

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