6pw7: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6pw7 is ON HOLD  until Paper Publication
+==X-ray crystal structure of C. elegans STIM EF-SAM domain==
+<StructureSection load='6pw7' size='340' side='right'caption='[[6pw7]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6pw7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PW7 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></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stim-1, Y55B1BM.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=6pw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pw7 OCA], [http://pdbe.org/6pw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pw7 RCSB], [http://www.ebi.ac.uk/pdbsum/6pw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pw7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/STIM1_CAEEL STIM1_CAEEL]] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor which upon Ca(2+) depletion, activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, orai-1. Essential for Ca (2+) and IP3-dependent contractile activity of gonad sheath cells and spermatheca. Essential for fertility. Does not play a role in posterior body wall muscle contraction (pBoc) rhythmicity, intestinal cell oscillatory Ca(2+) signaling or intestinal ER Ca(2+) hemeostasis.<ref>PMID:16966474</ref> <ref>PMID:17218360</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Store operated calcium (Ca(2+)) entry (SOCE) is the process whereby endoplasmic reticulum (ER) Ca(2+) store depletion causes Orai1-composed Ca(2+) channels on the plasma membrane (PM) to open, mediating a rise in cytosolic Ca(2+) levels. Stromal interaction molecules (STIM)s are the proteins that directly sense ER Ca(2+) content and gate Orai1 channels due to store depletion. The trigger for STIM activation is Ca(2+) unbinding from the ER lumen-oriented domains, which consist of a non-conserved amino (N) terminal region and EF-hand and sterile alpha motif (SAM) domains (EF-SAM), highly conserved from humans to Caenorhabditis elegans. Solution NMR structures of the human EF-SAM domains have been determined at high Ca(2+) concentrations; however, no direct structural view of the Ca(2+) binding mode has been elucidated. Further, no atomic resolution data currently exists on EF-SAM at low Ca(2+) levels. Here, we determined the X-ray crystal structure of the C. elegans STIM luminal domain, revealing that EF-SAM binds a single Ca(2+) ion with pentagonal bipyramidal geometry and an ancillary alpha-helix formed by the N-terminal region acts as a brace to stabilize EF-SAM. Using solution NMR, we observed EF-hand domain unfolding and a conformational exchange between folded and unfolded states involving the ancillary alpha-helix and the canonical EF-hand in low Ca(2+). Remarkably, we also detected an alpha-helix (+Ca(2+)) to beta-strand (-Ca(2+)) transition at the terminal SAM domain alpha-helix. Collectively, our analyses indicate that one canonically bound Ca(2+) ion is sufficient to stabilize the quiescent luminal domain structure, precluding unfolding, conformational exchange and secondary structure transformation.
-Authors:
+Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain.,Enomoto M, Nishikawa T, Back SI, Ishiyama N, Zheng L, Stathopulos PB, Ikura M J Mol Biol. 2019 Oct 15. pii: S0022-2836(19)30594-7. doi:, 10.1016/j.jmb.2019.10.003. PMID:31626806<ref>PMID:31626806</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6pw7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Caeel]]
+[[Category: Large Structures]]
+[[Category: Back, S I]]
+[[Category: Enomoto, M]]
+[[Category: Ikura, M]]
+[[Category: Ishiyama, N]]
+[[Category: Nishikawa, T]]
+[[Category: Stathopulos, P B]]
+[[Category: Zheng, L]]
+[[Category: Calcium release-activated channel]]
+[[Category: Ef-hand]]
+[[Category: Sam-domain]]
+[[Category: Signaling protein]]