2LQV
YebF
Summary for 2LQV
| Entry DOI | 10.2210/pdb2lqv/pdb |
| NMR Information | BMRB: 18332 |
| Descriptor | Protein yebF (1 entity in total) |
| Functional Keywords | secretion, protein transport |
| Biological source | Escherichia coli |
| Cellular location | Secreted: P33219 |
| Total number of polymer chains | 1 |
| Total formula weight | 11883.17 |
| Authors | Prehna, G.,Zhang, G.,Gong, X.,Duszyk, M.,Okon, M.,Mcintosh, L.P.,Weiner, J.H.,Strynadka, N.C.J. (deposition date: 2012-03-16, release date: 2012-06-13, Last modification date: 2023-06-14) |
| Primary citation | Prehna, G.,Zhang, G.,Gong, X.,Duszyk, M.,Okon, M.,McIntosh, L.P.,Weiner, J.H.,Strynadka, N.C. A Protein Export Pathway Involving Escherichia coli Porins. Structure, 20:1154-1166, 2012 Cited by PubMed Abstract: Escherichia coli export the protein YebF into the extracellular medium by a two-step process. However, as no general outer membrane protein secretion system common to all E. coli strains has been reported, the mechanism of export has remained unclear. Herein, we identify the outer membrane proteins OmpF, OmpC, and OmpX as central to the YebF export mechanism using both genetic and planar lipid bilayer experiments. The nuclear magnetic resonance structural ensemble of YebF reveals a cystatin-like fold consisting of a structured core and an extended dynamic surface in a state of conformational exchange. This surface, conserved throughout YebF orthologs of Enterobacteriaceae, may facilitate the porin-mediated transport of YebF as amino acid substitutions of dynamic residues reduced secretion to the extracellular medium. Our results demonstrate that OmpF and OmpC not only operate to import ions and protein toxins but may also contribute to the export of the YebF protein family. PubMed: 22658749DOI: 10.1016/j.str.2012.04.014 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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