6nq7: Difference between revisions
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<StructureSection load='6nq7' size='340' side='right'caption='[[6nq7]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='6nq7' size='340' side='right'caption='[[6nq7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6nq7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6nq7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NQ7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nq7 OCA], [https://pdbe.org/6nq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nq7 RCSB], [https://www.ebi.ac.uk/pdbsum/6nq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nq7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/YETJ_BACSU YETJ_BACSU] | |||
<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: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Chang Y]] | ||
[[Category: Guo | [[Category: Guo G]] | ||
[[Category: Liu | [[Category: Liu Q]] | ||
Latest revision as of 09:57, 11 October 2023
Crystal structure of YetJ from Bacillus Subtilis crystallized in lipidic cubic phaseCrystal structure of YetJ from Bacillus Subtilis crystallized in lipidic cubic phase
Structural highlights
FunctionPublication Abstract from PubMedThe anti-apoptotic transmembrane Bax inhibitor motif (TMBIM) containing protein family regulates Ca(2+) homeostasis, cell death, and the progression of diseases including cancers. The recent crystal structures of the TMBIM homolog BsYetJ reveal a conserved Asp171-Asp195 dyad that is proposed in regulating a pH-dependent Ca(2+) translocation. Here we show that BsYetJ mediates Ca(2+) fluxes in permeabilized mammalian cells, and its interaction with Ca(2+) is sensitive to protons and other cations. We report crystal structures of BsYetJ in additional states, revealing the flexibility of the dyad in a closed state and a pore-opening mechanism. Functional studies show that the dyad is responsible for both Ca(2+) affinity and pH dependence. Computational simulations suggest that protonation of Asp171 weakens its interaction with Arg60, leading to an open state. Our integrated analysis provides insights into the regulation of the BsYetJ Ca(2+) channel that may inform understanding of human TMBIM proteins regarding their roles in cell death and diseases. Ion and pH Sensitivity of a TMBIM Ca(2+) Channel.,Guo G, Xu M, Chang Y, Luyten T, Seitaj B, Liu W, Zhu P, Bultynck G, Shi L, Quick M, Liu Q Structure. 2019 Mar 15. pii: S0969-2126(19)30081-4. doi:, 10.1016/j.str.2019.03.003. PMID:30930064[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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