5M1U
Solution structure of CsgF in DHPC micelles
Summary for 5M1U
| Entry DOI | 10.2210/pdb5m1u/pdb |
| NMR Information | BMRB: 34052 |
| Descriptor | Curli production assembly/transport component CsgF (1 entity in total) |
| Functional Keywords | curli, type viii secretion system, intrinsically disordered protein, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane : P0AE98 |
| Total number of polymer chains | 1 |
| Total formula weight | 13947.13 |
| Authors | Spehr, J.,Schubeis, T.,Ahmed, M.,Ritter, C. (deposition date: 2016-10-10, release date: 2017-10-11, Last modification date: 2024-06-19) |
| Primary citation | Schubeis, T.,Spehr, J.,Viereck, J.,Kopping, L.,Nagaraj, M.,Ahmed, M.,Ritter, C. Structural and functional characterization of the Curli adaptor protein CsgF. FEBS Lett., 592:1020-1029, 2018 Cited by PubMed Abstract: Curli are functional amyloids that form a major part of the biofilm produced by many enterobacteriaceae. A multiprotein 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 dihexanoylphosphocholine micelles. Interestingly, CsgF contains large unstructured domains and does not show a globular fold. The data presented shed new light on the molecular mechanism of Curli amyloid surface attachment. PubMed: 29427517DOI: 10.1002/1873-3468.13002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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