6si7: Difference between revisions

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New page: '''Unreleased structure''' The entry 6si7 is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6si7 is ON HOLD
==Structure of the curli secretion-assembly complex CsgG:CsgF==
<StructureSection load='6si7' size='340' side='right'caption='[[6si7]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6si7]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SI7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=6si7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6si7 OCA], [https://pdbe.org/6si7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6si7 RCSB], [https://www.ebi.ac.uk/pdbsum/6si7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6si7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CSGF_ECOLI CSGF_ECOLI]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Single-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35-residue N-terminal region of its extracellular interaction partner CsgF to produce a dual-constriction pore with improved signal and base-calling accuracy for homopolymer regions. The electron cryo-microscopy structure of CsgG in complex with full-length CsgF shows that the 33 N-terminal residues of CsgF bind inside the beta-barrel of the pore, forming a defined second constriction. In complexes of CsgG bound to a 35-residue CsgF constriction peptide, the second constriction is separated from the primary constriction by ~25 A. We find that both constrictions contribute to electrical signal modulation during single-stranded DNA translocation. DNA sequencing using a prototype CsgG-CsgF protein pore with two constrictions improved single-read accuracy by 25 to 70% in homopolymers up to 9 nucleotides long.


Authors:  
A dual-constriction biological nanopore resolves homonucleotide sequences with high fidelity.,Van der Verren SE, Van Gerven N, Jonckheere W, Hambley R, Singh P, Kilgour J, Jordan M, Wallace EJ, Jayasinghe L, Remaut H Nat Biotechnol. 2020 Jul 6. pii: 10.1038/s41587-020-0570-8. doi:, 10.1038/s41587-020-0570-8. PMID:32632300<ref>PMID:32632300</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6si7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Remaut H]]
[[Category: Van der Verren SE]]
Retrieved from "https://proteopedia.org/6si7"