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==NMR structure of the Bak transmembrane helix in lipid nanodiscs==
==NMR structure of the Bak transmembrane helix in lipid nanodiscs==
<StructureSection load='7ofo' size='340' side='right'caption='[[7ofo]]' scene=''>
<StructureSection load='7ofo' size='340' side='right'caption='[[7ofo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OFO FirstGlance]. <br>
<table><tr><td colspan='2'>[[7ofo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OFO FirstGlance]. <br>
</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=7ofo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofo OCA], [https://pdbe.org/7ofo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofo RCSB], [https://www.ebi.ac.uk/pdbsum/7ofo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofo ProSAT]</span></td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7ofm|7ofm]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAK1, BAK, BCL2L7, CDN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=7ofo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofo OCA], [https://pdbe.org/7ofo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofo RCSB], [https://www.ebi.ac.uk/pdbsum/7ofo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/BAK_HUMAN BAK_HUMAN]] In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.<ref>PMID:8521816</ref> <ref>PMID:17157251</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Permeabilization of the outer mitochondrial membrane by pore-forming Bcl2 proteins is a crucial step for the induction of apoptosis. Despite a large set of data suggesting global conformational changes within pro-apoptotic Bak during pore formation, high-resolution structural details in a membrane environment remain sparse. Here, we used NMR and HDX-MS (Hydrogen deuterium exchange mass spectrometry) in lipid nanodiscs to gain important high-resolution structural insights into the conformational changes of Bak at the membrane that are dependent on a direct activation by BH3-only proteins. Furthermore, we determined the first high-resolution structure of the Bak transmembrane helix. Upon activation, alpha-helix 1 in the soluble domain of Bak dissociates from the protein and adopts an unfolded and dynamic potentially membrane-bound state. In line with this finding, comparative protein folding experiments with Bak and anti-apoptotic BclxL suggest that alpha-helix 1 in Bak is a metastable structural element contributing to its pro-apoptotic features. Consequently, mutagenesis experiments aimed at stabilizing alpha-helix 1 yielded Bak variants with delayed pore-forming activity. These insights will contribute to a better mechanistic understanding of Bak-mediated membrane permeabilization.
High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane.,Sperl LE, Ruhrnossl F, Schiller A, Haslbeck M, Hagn F EMBO J. 2021 Oct 18;40(20):e107159. doi: 10.15252/embj.2020107159. Epub 2021 Sep , 15. PMID:34523144<ref>PMID:34523144</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ofo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hagn F]]
[[Category: Hagn, F]]
[[Category: Sperl LE]]
[[Category: Sperl, L E]]
[[Category: Apoptosis]]
[[Category: Bcl2 protein]]
[[Category: Mitochondria]]
[[Category: Pore formation]]
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