5m1u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of CsgF in DHPC micelles== | |
| + | <StructureSection load='5m1u' size='340' side='right'caption='[[5m1u]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M1U FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5m1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1u OCA], [https://pdbe.org/5m1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m1u RCSB], [https://www.ebi.ac.uk/pdbsum/5m1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CSGF_ECOLI CSGF_ECOLI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Curli are functional amyloids that form a major part of the biofilm produced by many enterobacteriaceae. A multi protein system around the outer membrane protein CsgG is in charge of the export and controlled propagation of the main Curli subunits, CsgA and CsgB. CsgF is essential for the linkage of the main amyloid-forming proteins to the cell surface. Here, we present a profound biochemical and biophysical characterization of recombinant CsgF, highlighted by a solution NMR structure of CsgF in the presence of DHPC micelles. Interestingly, CsgF contains large unstructured domains and does not show a globular fold. The data presented sheds new light on the molecular mechanism of Curli amyloid surface attachment. This article is protected by copyright. All rights reserved. | ||
| - | + | Structural and functional characterization of the Curli adaptor protein CsgF.,Schubeis T, Spehr J, Viereck J, Kopping L, Nagaraj M, Ahmed M, Ritter C FEBS Lett. 2018 Feb 10. doi: 10.1002/1873-3468.13002. PMID:29427517<ref>PMID:29427517</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5m1u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ahmed M]] | ||
| + | [[Category: Ritter C]] | ||
| + | [[Category: Schubeis T]] | ||
| + | [[Category: Spehr J]] | ||
Current revision
Solution structure of CsgF in DHPC micelles
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