5gql: Difference between revisions
New page: '''Unreleased structure''' The entry 5gql is ON HOLD Authors: Abe, S., Tabe, H., Ijiri, H., Yamashita, K., Hirata, K., Mori, H., Ueno, T. Description: Crystal structure of Wild Type Cy... |
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The entry | ==Crystal structure of Wild Type Cypovirus Polyhedra== | ||
<StructureSection load='5gql' size='340' side='right'caption='[[5gql]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gql]] 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=5GQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GQL 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]] 1.78Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gql OCA], [https://pdbe.org/5gql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gql RCSB], [https://www.ebi.ac.uk/pdbsum/5gql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gql 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 == | |||
Crystalline porous materials have been investigated for development of important applications in molecular storage, separations, and catalysis. The potential of protein crystals is increasing as they become better understood. Protein crystals have been regarded as porous materials because they present highly ordered 3D arrangements of protein molecules with high porosity and wide range of pore sizes. However, it remains difficult to functionalize protein crystals in living cells. Here, we report that polyhedra, a natural crystalline protein assembly of polyhedrin monomer (PhM) produced in insect cells infected by cypovirus, can be engineered to extend porous networks by deleting selected amino acid residues located on the intermolecular contact region of PhM. The adsorption rates and quantities of fluorescent dyes stored within the mutant crystals are increased relative to those of the wild-type polyhedra crystal (WTPhC) under both in vitro and in vivo conditions. These results provide a strategy for designing self-assembled protein materials with applications in molecular recognition and storage of exogenous substances in living cell as well as an entry point for development of bioorthogonal chemistry and in vivo crystal structure analysis. | |||
Crystal Engineering of Self-Assembled Porous Protein Materials in Living Cells.,Abe S, Tabe H, Ijiri H, Yamashita K, Hirata K, Atsumi K, Shimoi T, Akai M, Mori H, Kitagawa S, Ueno T ACS Nano. 2017 Feb 9. doi: 10.1021/acsnano.6b06099. PMID:28094987<ref>PMID:28094987</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5gql" style="background-color:#fffaf0;"></div> | ||
[[Category: Hirata | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Polyhedrin|Polyhedrin]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Bombyx mori cypovirus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: Abe S]] | |||
[[Category: Hirata K]] | |||
[[Category: Ijiri H]] | |||
[[Category: Mori H]] | |||
[[Category: Tabe H]] | |||
[[Category: Ueno T]] | |||
[[Category: Yamashita K]] | |||
Latest revision as of 14:39, 2 August 2023
Crystal structure of Wild Type Cypovirus PolyhedraCrystal structure of Wild Type Cypovirus Polyhedra
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 PubMedCrystalline porous materials have been investigated for development of important applications in molecular storage, separations, and catalysis. The potential of protein crystals is increasing as they become better understood. Protein crystals have been regarded as porous materials because they present highly ordered 3D arrangements of protein molecules with high porosity and wide range of pore sizes. However, it remains difficult to functionalize protein crystals in living cells. Here, we report that polyhedra, a natural crystalline protein assembly of polyhedrin monomer (PhM) produced in insect cells infected by cypovirus, can be engineered to extend porous networks by deleting selected amino acid residues located on the intermolecular contact region of PhM. The adsorption rates and quantities of fluorescent dyes stored within the mutant crystals are increased relative to those of the wild-type polyhedra crystal (WTPhC) under both in vitro and in vivo conditions. These results provide a strategy for designing self-assembled protein materials with applications in molecular recognition and storage of exogenous substances in living cell as well as an entry point for development of bioorthogonal chemistry and in vivo crystal structure analysis. Crystal Engineering of Self-Assembled Porous Protein Materials in Living Cells.,Abe S, Tabe H, Ijiri H, Yamashita K, Hirata K, Atsumi K, Shimoi T, Akai M, Mori H, Kitagawa S, Ueno T ACS Nano. 2017 Feb 9. doi: 10.1021/acsnano.6b06099. PMID:28094987[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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