View source for 5efm


==Beclin 1 Flexible-helical Domian (FHD) (141-171)==
<StructureSection load='5efm' size='340' side='right'caption='[[5efm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5efm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFM 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]] 1.95&#8491;</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=5efm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efm OCA], [https://pdbe.org/5efm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efm RCSB], [https://www.ebi.ac.uk/pdbsum/5efm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BECN1 is essential for autophagy, a critical eukaryotic cellular homeostasis pathway. Here we delineate a highly conserved BECN1 domain located between previously characterized BH3 and coiled-coil domains and elucidate its structure and role in autophagy. The 2.0 A sulfur-single-wavelength anomalous dispersion X-ray crystal structure of this domain demonstrates that its N-terminal half is unstructured while its C-terminal half is helical; hence, we name it the flexible helical domain (FHD). Circular dichroism spectroscopy, double electron-electron resonance-electron paramagnetic resonance, and small-angle X-ray scattering (SAXS) analyses confirm that the FHD is partially disordered, even in the context of adjacent BECN1 domains. Molecular dynamic simulations fitted to SAXS data indicate that the FHD transiently samples more helical conformations. FHD helicity increases in 2,2,2-trifluoroethanol, suggesting it may become more helical upon binding. Lastly, cellular studies show that conserved FHD residues are required for starvation-induced autophagy. Thus, the FHD likely undergoes a binding-associated disorder-to-helix transition, and conserved residues critical for this interaction are essential for starvation-induced autophagy.

Conformational Flexibility Enables the Function of a BECN1 Region Essential for Starvation-Mediated Autophagy.,Mei Y, Ramanathan A, Glover K, Stanley C, Sanishvili R, Chakravarthy S, Yang Z, Colbert CL, Sinha SC Biochemistry. 2016 Apr 5;55(13):1945-58. doi: 10.1021/acs.biochem.5b01264. Epub, 2016 Mar 21. PMID:26937551<ref>PMID:26937551</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5efm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mei Y]]
[[Category: Sinha S]]