5yrb: Difference between revisions
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==Crystal Structure of Oxidized Cypovirus Polyhedra R13A/E73C/Y83C/S193C/A194C Mutant== | |||
<StructureSection load='5yrb' size='340' side='right'caption='[[5yrb]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5yrb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YRB 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5yrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yrb OCA], [https://pdbe.org/5yrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yrb RCSB], [https://www.ebi.ac.uk/pdbsum/5yrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yrb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PYHD_CPVBM PYHD_CPVBM] 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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein crystals are formed via ordered arrangements of proteins, which assemble to form supramolecular structures. Here, we show a method for the assembly of supramolecular protein cages within a crystalline environment. The cages are stabilized by covalent cross-linking allowing their release via dissolution of the crystal. The high stability of the desiccated protein crystals allows cages to be constructed. | |||
Supramolecular protein cages constructed from a crystalline protein matrix.,Negishi H, Abe S, Yamashita K, Hirata K, Niwase K, Boudes M, Coulibaly F, Mori H, Ueno T Chem Commun (Camb). 2018 Feb 20;54(16):1988-1991. doi: 10.1039/c7cc08689j. PMID:29405208<ref>PMID:29405208</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5yrb" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Boudes | ==See Also== | ||
[[Category: | *[[Polyhedrin|Polyhedrin]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Ueno | [[Category: Bombyx mori cypovirus 1]] | ||
[[Category: Large Structures]] | |||
[[Category: Abe S]] | |||
[[Category: Boudes M]] | |||
[[Category: Coulibaly F]] | |||
[[Category: Hirata K]] | |||
[[Category: Mori H]] | |||
[[Category: Negishi H]] | |||
[[Category: Niwase K]] | |||
[[Category: Ueno T]] | |||
[[Category: Yamashita K]] | |||
Latest revision as of 07:59, 21 November 2024
Crystal Structure of Oxidized Cypovirus Polyhedra R13A/E73C/Y83C/S193C/A194C MutantCrystal Structure of Oxidized Cypovirus Polyhedra R13A/E73C/Y83C/S193C/A194C Mutant
Structural highlights
FunctionPYHD_CPVBM 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. Publication Abstract from PubMedProtein crystals are formed via ordered arrangements of proteins, which assemble to form supramolecular structures. Here, we show a method for the assembly of supramolecular protein cages within a crystalline environment. The cages are stabilized by covalent cross-linking allowing their release via dissolution of the crystal. The high stability of the desiccated protein crystals allows cages to be constructed. Supramolecular protein cages constructed from a crystalline protein matrix.,Negishi H, Abe S, Yamashita K, Hirata K, Niwase K, Boudes M, Coulibaly F, Mori H, Ueno T Chem Commun (Camb). 2018 Feb 20;54(16):1988-1991. doi: 10.1039/c7cc08689j. PMID:29405208[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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