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| - | ==THE X-RAY STRUCTURE OF THE SORCIN CALCIUM BINDING DOMAIN (SCBD) PROVIDES INSIGHT INTO THE PHOSPHORYLATION AND CALCIUM DEPENDENT PROCESSESS== | + | |
| - | <StructureSection load='1gjy' size='340' side='right' caption='[[1gjy]], [[Resolution|resolution]] 2.20Å' scene=''> | + | ==The X-ray structure of the Sorcin Calcium Binding Domain (SCBD) provides insight into the phosphorylation and calcium dependent processess== |
| | + | <StructureSection load='1gjy' size='340' side='right'caption='[[1gjy]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gjy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gjy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</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=1gjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjy OCA], [http://pdbe.org/1gjy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjy RCSB], [http://www.ebi.ac.uk/pdbsum/1gjy PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1gjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjy OCA], [https://pdbe.org/1gjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjy RCSB], [https://www.ebi.ac.uk/pdbsum/1gjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SORCN_CRIGR SORCN_CRIGR] Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the sarcoplasmic reticulum in the heart. Modulates the activity of RYR2 calcium channels.<ref>PMID:15754088</ref> <ref>PMID:17029407</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/1gjy_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/1gjy_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Cricetulus griseus]] | | [[Category: Cricetulus griseus]] |
| - | [[Category: Chiancone, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Ilari, A]] | + | [[Category: Chiancone E]] |
| - | [[Category: Johnson, K A]] | + | [[Category: Ilari A]] |
| - | [[Category: Nastopoulos, V]] | + | [[Category: Johnson KA]] |
| - | [[Category: Tsernoglou, D]] | + | [[Category: Nastopoulos V]] |
| - | [[Category: Calcium binding]]
| + | [[Category: Tsernoglou D]] |
| - | [[Category: Calcium-binding]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| Structural highlights
Function
SORCN_CRIGR Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the sarcoplasmic reticulum in the heart. Modulates the activity of RYR2 calcium channels.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Sorcin is a 21.6 kDa calcium binding protein, expressed in a number of mammalian tissues that belongs to the small, recently identified penta-EF-hand (PEF) family. Like all members of this family, sorcin undergoes a Ca2+-dependent translocation from cytosol to membranes where it binds to target proteins. For sorcin, the targets differ in different tissues, indicating that it takes part in a number of Ca2+-regulated processes. The sorcin monomer is organized in two domains like in all PEF proteins: a flexible, hydrophobic, glycine-rich N-terminal region and a calcium binding C-terminal domain. In vitro, the PEF proteins are dimeric in their Ca2+-free form, but have a marked tendency to precipitate when bound to calcium. Stabilization of the dimeric structure is achieved by pairing of the uneven EF-hand, EF5. Sorcin can also form tetramers at acid pH.The sorcin calcium binding domain (SCBD, residues 33-198) expressed in Escherichia coli was crystallized in the Ca2+-free form. The structure was solved by molecular replacement and was refined to 2.2 A with a crystallographic R-factor of 22.4 %. Interestingly, the asymmetric unit contains two dimers.The structure of the SCBD leads to a model that explains the solution properties and describes the Ca2+-induced conformational changes. Phosphorylation studies show that the N-terminal domain hinders phosphorylation of SCBD, i.e. the rate of phosphorylation increased twofold in the absence of the N-terminal region. In addition, previous fluorescence studies indicated that hydrophobic residues are exposed to solvent upon Ca2+ binding to full-length sorcin. The model accounts for these data by proposing that Ca2+ binding weakens the interactions between the two domains and leads to their reorientation, which exposes hydrophobic regions facilitating the Ca2+-dependent binding to target proteins at or near membranes.
The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein.,Ilari A, Johnson KA, Nastopoulos V, Verzili D, Zamparelli C, Colotti G, Tsernoglou D, Chiancone E J Mol Biol. 2002 Mar 29;317(3):447-58. PMID:11922676[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsumoto T, Hisamatsu Y, Ohkusa T, Inoue N, Sato T, Suzuki S, Ikeda Y, Matsuzaki M. Sorcin interacts with sarcoplasmic reticulum Ca(2+)-ATPase and modulates excitation-contraction coupling in the heart. Basic Res Cardiol. 2005 May;100(3):250-62. PMID:15754088 doi:10.1007/s00395-005-0518-7
- ↑ Colotti G, Zamparelli C, Verzili D, Mella M, Loughrey CM, Smith GL, Chiancone E. The W105G and W99G sorcin mutants demonstrate the role of the D helix in the Ca(2+)-dependent interaction with annexin VII and the cardiac ryanodine receptor. Biochemistry. 2006 Oct 17;45(41):12519-29. PMID:17029407 doi:10.1021/bi060416a
- ↑ Ilari A, Johnson KA, Nastopoulos V, Verzili D, Zamparelli C, Colotti G, Tsernoglou D, Chiancone E. The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein. J Mol Biol. 2002 Mar 29;317(3):447-58. PMID:11922676 doi:10.1006/jmbi.2002.5417
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