2wux: Difference between revisions
No edit summary |
No edit summary |
||
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==the crystal structure of recombinant baculovirus polyhedra== | |||
<StructureSection load='2wux' size='340' side='right'caption='[[2wux]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WUX FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wuy|2wuy]]</div></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=2wux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wux OCA], [https://pdbe.org/2wux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wux RCSB], [https://www.ebi.ac.uk/pdbsum/2wux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wux ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/PYHD_NPVAC PYHD_NPVAC]] Major component of the virus occlusion bodies, which are large proteinaceous structures (polyhedra), that protect the virus from the outside environment for extended periods until they are ingested by insect larvae. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/2wux_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wux ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Natural protein crystals (polyhedra) armour certain viruses, allowing them to survive for years under hostile conditions. We have determined the structure of polyhedra of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), revealing a highly symmetrical covalently cross-braced robust lattice, the subunits of which possess a flexible adaptor enabling this supra-molecular assembly to specifically entrap massive baculoviruses. Inter-subunit chemical switches modulate the controlled release of virus particles in the unusual high pH environment of the target insect's gut. Surprisingly, the polyhedrin subunits are more similar to picornavirus coat proteins than to the polyhedrin of cytoplasmic polyhedrosis virus (CPV). It is, therefore, remarkable that both AcMNPV and CPV polyhedra possess identical crystal lattices and crystal symmetry. This crystalline arrangement must be particularly well suited to the functional requirements of the polyhedra and has been either preserved or re-selected during evolution. The use of flexible adaptors to generate a powerful system for packaging irregular particles is characteristic of the AcMNPV polyhedrin and may provide a vehicle to sequester a wide range of objects such as biological nano-particles. | |||
How baculovirus polyhedra fit square pegs into round holes to robustly package viruses.,Ji X, Sutton G, Evans G, Axford D, Owen R, Stuart DI EMBO J. 2010 Jan 20;29(2):505-14. Epub 2009 Dec 3. PMID:19959989<ref>PMID:19959989</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2wux" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Polyhedrin|Polyhedrin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Axford, D | [[Category: Acmnpv]] | ||
[[Category: Evans, G | [[Category: Large Structures]] | ||
[[Category: Ji, X | [[Category: Axford, D]] | ||
[[Category: Owen, R | [[Category: Evans, G]] | ||
[[Category: Stuart, D I | [[Category: Ji, X]] | ||
[[Category: Sutton, G | [[Category: Owen, R]] | ||
[[Category: Stuart, D I]] | |||
[[Category: Sutton, G]] | |||
[[Category: Microcrystal]] | [[Category: Microcrystal]] | ||
[[Category: Polyhedra]] | [[Category: Polyhedra]] | ||
Latest revision as of 13:40, 13 April 2022
the crystal structure of recombinant baculovirus polyhedrathe crystal structure of recombinant baculovirus polyhedra
Structural highlights
Function[PYHD_NPVAC] Major component of the virus occlusion bodies, which are large proteinaceous structures (polyhedra), that protect the virus from the outside environment for extended periods until they are ingested by insect larvae. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNatural protein crystals (polyhedra) armour certain viruses, allowing them to survive for years under hostile conditions. We have determined the structure of polyhedra of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), revealing a highly symmetrical covalently cross-braced robust lattice, the subunits of which possess a flexible adaptor enabling this supra-molecular assembly to specifically entrap massive baculoviruses. Inter-subunit chemical switches modulate the controlled release of virus particles in the unusual high pH environment of the target insect's gut. Surprisingly, the polyhedrin subunits are more similar to picornavirus coat proteins than to the polyhedrin of cytoplasmic polyhedrosis virus (CPV). It is, therefore, remarkable that both AcMNPV and CPV polyhedra possess identical crystal lattices and crystal symmetry. This crystalline arrangement must be particularly well suited to the functional requirements of the polyhedra and has been either preserved or re-selected during evolution. The use of flexible adaptors to generate a powerful system for packaging irregular particles is characteristic of the AcMNPV polyhedrin and may provide a vehicle to sequester a wide range of objects such as biological nano-particles. How baculovirus polyhedra fit square pegs into round holes to robustly package viruses.,Ji X, Sutton G, Evans G, Axford D, Owen R, Stuart DI EMBO J. 2010 Jan 20;29(2):505-14. Epub 2009 Dec 3. PMID:19959989[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||