4ldd: Difference between revisions
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==Crystal Structure of Ebola virus VP40 Hexamer== | |||
=== | <StructureSection load='4ldd' size='340' side='right' caption='[[4ldd]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ldd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Zebov Zebov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LDD FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ld8|4ld8]], [[4ldb|4ldb]], [[4ldi|4ldi]], [[4ldm|4ldm]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186538 ZEBOV])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ldd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ldd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ldd RCSB], [http://www.ebi.ac.uk/pdbsum/4ldd PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multilayered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle and demonstrate how a single wild-type, unmodified polypeptide can assemble into different structures for different functions. PAPERFLICK: | |||
Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle.,Bornholdt ZA, Noda T, Abelson DM, Halfmann P, Wood MR, Kawaoka Y, Saphire EO Cell. 2013 Aug 15;154(4):763-74. doi: 10.1016/j.cell.2013.07.015. PMID:23953110<ref>PMID:23953110</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Zebov]] | |||
[[Category: Ableson, D M.]] | [[Category: Ableson, D M.]] | ||
[[Category: Bornholdt, Z A.]] | [[Category: Bornholdt, Z A.]] | ||
Revision as of 08:28, 24 September 2014
Crystal Structure of Ebola virus VP40 HexamerCrystal Structure of Ebola virus VP40 Hexamer
Structural highlights
Publication Abstract from PubMedProteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multilayered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle and demonstrate how a single wild-type, unmodified polypeptide can assemble into different structures for different functions. PAPERFLICK: Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle.,Bornholdt ZA, Noda T, Abelson DM, Halfmann P, Wood MR, Kawaoka Y, Saphire EO Cell. 2013 Aug 15;154(4):763-74. doi: 10.1016/j.cell.2013.07.015. PMID:23953110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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