6suq
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6suq is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of TcdB2-TccC3-TEV== | |
| + | <StructureSection load='6suq' size='340' side='right'caption='[[6suq]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6suq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_luminescens Photorhabdus luminescens] and [https://en.wikipedia.org/wiki/Tobacco_etch_virus Tobacco etch virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SUQ 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]] 3.7Å</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=6suq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6suq OCA], [https://pdbe.org/6suq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6suq RCSB], [https://www.ebi.ac.uk/pdbsum/6suq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6suq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8GF97_PHOLU Q8GF97_PHOLU] [https://www.uniprot.org/uniprot/Q8GF99_PHOLU Q8GF99_PHOLU] [https://www.uniprot.org/uniprot/POLG_TEV POLG_TEV] Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> Both 6K peptides are indispensable for virus replication (By similarity).<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> Nuclear inclusion protein A: has RNA-binding and proteolytic activities.<ref>PMID:9880030</ref> <ref>PMID:11414807</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme varies between Tc toxins from different species and is not conserved. Here, we investigate whether the toxic enzyme can be replaced by other small proteins of different origin and properties, namely Cdc42, herpes simplex virus ICP47, Arabidopsis thaliana iLOV, Escherichia coli DHFR, Ras-binding domain of CRAF kinase, and TEV protease. Using a combination of electron microscopy, X-ray crystallography and in vitro translocation assays, we demonstrate that it is possible to turn Tc toxins into customizable molecular syringes for delivering proteins of interest across membranes. We also infer the guidelines that protein cargos must obey in terms of size, charge, and fold in order to apply Tc toxins as a universal protein translocation system. | ||
| - | + | Towards the application of Tc toxins as a universal protein translocation system.,Roderer D, Schubert E, Sitsel O, Raunser S Nat Commun. 2019 Nov 20;10(1):5263. doi: 10.1038/s41467-019-13253-8. PMID:31748551<ref>PMID:31748551</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6suq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Photorhabdus luminescens]] | ||
| + | [[Category: Tobacco etch virus]] | ||
| + | [[Category: Raunser S]] | ||
| + | [[Category: Roderer D]] | ||
| + | [[Category: Schubert E]] | ||
| + | [[Category: Sitsel O]] | ||
Current revision
Crystal Structure of TcdB2-TccC3-TEV
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