6tzc: Difference between revisions
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==Crystal Structure of African Swine Fever Virus A179L with the Autophagy Regulator Beclin== | |||
<StructureSection load='6tzc' size='340' side='right'caption='[[6tzc]], [[Resolution|resolution]] 2.41Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6tzc]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TZC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></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=6tzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tzc OCA], [http://pdbe.org/6tzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tzc RCSB], [http://www.ebi.ac.uk/pdbsum/6tzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tzc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. [[http://www.uniprot.org/uniprot/BECN1_PIG BECN1_PIG]] Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).[UniProtKB:O88597][UniProtKB:Q14457][UniProtKB:Q91XJ1] Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors.[UniProtKB:O88597][UniProtKB:Q14457] [[http://www.uniprot.org/uniprot/ARBH_ASFB7 ARBH_ASFB7]] Suppresses apoptosis in host cell and thus facilitates production of progeny virions (PubMed:9123849, PubMed:18329683). Has the ability to potentially bind to all the members of the proapoptotic Bcl-2 family (PubMed:28053104, PubMed:18329683).<ref>PMID:18329683</ref> <ref>PMID:28053104</ref> <ref>PMID:9123849</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Subversion of programmed cell death-based host defence systems is a prominent feature of infections by large DNA viruses. African swine fever virus (ASFV) is a large DNA virus and sole member of the Asfarviridae family that harbours the B-cell lymphoma 2 or Bcl-2 homolog A179L. A179L has been shown to bind to a range of cell death-inducing host proteins, including pro-apoptotic Bcl-2 proteins as well as the autophagy regulator Beclin. Here we report the crystal structure of A179L bound to the Beclin BH3 motif. A179L engages Beclin using the same canonical ligand-binding groove that is utilized to bind to pro-apoptotic Bcl-2 proteins. The mode of binding of Beclin to A179L mirrors that of Beclin binding to human Bcl-2 and Bcl-xL as well as murine gamma-herpesvirus 68. The introduction of bulky hydrophobic residues into the A179L ligand-binding groove via site-directed mutagenesis ablates binding of Beclin to A179L, leading to a loss of the ability of A179L to modulate autophagosome formation in Vero cells during starvation. Our findings provide a mechanistic understanding for the potent autophagy inhibitory activity of A179L and serve as a platform for more detailed investigations into the role of autophagy during ASFV infection. | |||
Crystal Structure of African Swine Fever Virus A179L with the Autophagy Regulator Beclin.,Banjara S, Shimmon GL, Dixon LK, Netherton CL, Hinds MG, Kvansakul M Viruses. 2019 Aug 27;11(9). pii: v11090789. doi: 10.3390/v11090789. PMID:31461953<ref>PMID:31461953</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6tzc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Banjara, S]] | |||
[[Category: Hinds, M G]] | |||
[[Category: Kvansakul, M]] | |||
[[Category: Apoptosis]] | |||
[[Category: Autophagy]] | |||
[[Category: Bcl-2 virus]] | |||
[[Category: Structural protein]] | |||
[[Category: Structural protein-apoptosis complex]] | |||
