View source for 4pgu


==Crystal structure of YetJ from Bacillus Subtilis at pH 7 by soaking==
<StructureSection load='4pgu' size='340' side='right'caption='[[4pgu]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pgu]] 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=4PGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PGU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.401&#8491;</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=4pgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgu OCA], [https://pdbe.org/4pgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pgu RCSB], [https://www.ebi.ac.uk/pdbsum/4pgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pgu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YETJ_BACSU YETJ_BACSU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calcium homeostasis balances passive calcium leak and active calcium uptake. Human Bax inhibitor-1 (hBI-1) is an antiapoptotic protein that mediates a calcium leak and is representative of a highly conserved and widely distributed family, the transmembrane Bax inhibitor motif (TMBIM) proteins. Here, we present crystal structures of a bacterial homolog and characterize its calcium leak activity. The structure has a seven-transmembrane-helix fold that features two triple-helix sandwiches wrapped around a central C-terminal helix. Structures obtained in closed and open conformations are reversibly interconvertible by change of pH. A hydrogen-bonded, pKa (where Ka is the acid dissociation constant)-perturbed pair of conserved aspartate residues explains the pH dependence of this transition, and biochemical studies show that pH regulates calcium influx in proteoliposomes. Homology models for hBI-1 provide insights into TMBIM-mediated calcium leak and cytoprotective activity.

Structural basis for a pH-sensitive calcium leak across membranes.,Chang Y, Bruni R, Kloss B, Assur Z, Kloppmann E, Rost B, Hendrickson WA, Liu Q Science. 2014 Jun 6;344(6188):1131-5. doi: 10.1126/science.1252043. PMID:24904158<ref>PMID:24904158</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pgu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Chang Y]]
[[Category: Hendrickson WA]]
[[Category: Liu Q]]