5yhb: Difference between revisions
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==Crystal structure of Pd(allyl)/polyhedra mutant with deletion of Gly192-Ala194== | |||
<StructureSection load='5yhb' size='340' side='right' caption='[[5yhb]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5yhb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YHB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YHB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PD:PALLADIUM+ION'>PD</scene>, <scene name='pdbligand=PLL:PALLADIUM(II)+ALLYL+COMPLEX'>PLL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=5yhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhb OCA], [http://pdbe.org/5yhb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yhb RCSB], [http://www.ebi.ac.uk/pdbsum/5yhb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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 == | |||
The molecular structures of in cell protein crystals containing organometallic Pd(allyl) complexes were determined by performing microfocus X-ray diffraction experiments. The coordination sites in a polyhedrin mutant with deletion of selected amino acid residues located at the interface of the polyhedrin trimer are dramatically altered compared to those of the wild-type composite. | |||
Structure of in cell protein crystals containing organometallic complexes.,Abe S, Atsumi K, Yamashita K, Hirata K, Mori H, Ueno T Phys Chem Chem Phys. 2017 Nov 15. doi: 10.1039/c7cp06651a. PMID:29138769<ref>PMID:29138769</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5yhb" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Abe, S]] | |||
[[Category: Atsumi, K]] | [[Category: Atsumi, K]] | ||
[[Category: Hirata, K]] | [[Category: Hirata, K]] | ||
[[Category: Mori, H]] | |||
[[Category: Ueno, T]] | [[Category: Ueno, T]] | ||
[[Category: Yamashita, K]] | |||
[[Category: In vivo protein crystal]] | |||
[[Category: Metal complex]] | |||
[[Category: Polyhedra]] | |||
[[Category: Viral protein]] |
Revision as of 09:14, 29 November 2017
Crystal structure of Pd(allyl)/polyhedra mutant with deletion of Gly192-Ala194Crystal structure of Pd(allyl)/polyhedra mutant with deletion of Gly192-Ala194
Structural highlights
Function[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. Publication Abstract from PubMedThe molecular structures of in cell protein crystals containing organometallic Pd(allyl) complexes were determined by performing microfocus X-ray diffraction experiments. The coordination sites in a polyhedrin mutant with deletion of selected amino acid residues located at the interface of the polyhedrin trimer are dramatically altered compared to those of the wild-type composite. Structure of in cell protein crystals containing organometallic complexes.,Abe S, Atsumi K, Yamashita K, Hirata K, Mori H, Ueno T Phys Chem Chem Phys. 2017 Nov 15. doi: 10.1039/c7cp06651a. PMID:29138769[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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