6si7
From Proteopedia
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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''' | ||
| - | + | ==Structure of the curli secretion-assembly complex CsgG:CsgF== | |
| + | <StructureSection load='6si7' size='340' side='right'caption='[[6si7]], [[Resolution|resolution]] 3.40Å' 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]] 3.4Å</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </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]] | ||
Current revision
Structure of the curli secretion-assembly complex CsgG:CsgF
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