|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the coiled coil domain of Beclin 1, an essential autophagy protein== | | ==Crystal structure of the coiled coil domain of Beclin 1, an essential autophagy protein== |
| - | <StructureSection load='3q8t' size='340' side='right' caption='[[3q8t]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3q8t' size='340' side='right'caption='[[3q8t]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q8t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q8T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q8T FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Becn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=3q8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q8t OCA], [http://pdbe.org/3q8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q8t RCSB], [http://www.ebi.ac.uk/pdbsum/3q8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q8t ProSAT]</span></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=3q8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q8t OCA], [https://pdbe.org/3q8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q8t RCSB], [https://www.ebi.ac.uk/pdbsum/3q8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q8t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BECN1_RAT BECN1_RAT]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense (By similarity). | + | [https://www.uniprot.org/uniprot/BECN1_RAT BECN1_RAT] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense (By similarity). |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L- and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings at its coiled coil interface. Atg14L and UVRAG promote the transition of metastable homodimeric Beclin 1 to heterodimeric Beclin1-Atg14L/UVRAG assembly. Beclin 1 mutants with their 'imperfect' a-d' pairings modified to enhance self-interaction, show distinctively altered interactions with Atg14L or UVRAG. These results suggest that specific utilization of the dimer interface and modulation of the homodimer-heterodimer transition by Beclin 1-interacting partners may underlie the molecular mechanism that controls the formation of various Beclin1-VPS34 subcomplexes to exert their effect on an array of VPS34-related activities, including autophagy.
| + | |
| - | | + | |
| - | Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG.,Li X, He L, Che KH, Funderburk SF, Pan L, Pan N, Zhang M, Yue Z, Zhao Y Nat Commun. 2012 Feb 7;3:662. doi: 10.1038/ncomms1648. PMID:22314358<ref>PMID:22314358</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3q8t" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, X]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Zhao, Y]] | + | [[Category: Li X]] |
| - | [[Category: Apoptosis]] | + | [[Category: Zhao Y]] |
| - | [[Category: Atg14l uvrag]]
| + | |
| - | [[Category: Autophagy]]
| + | |
