2LQV
YebF
2LQV の概要
エントリーDOI | 10.2210/pdb2lqv/pdb |
NMR情報 | BMRB: 18332 |
分子名称 | Protein yebF (1 entity in total) |
機能のキーワード | secretion, protein transport |
由来する生物種 | Escherichia coli |
細胞内の位置 | Secreted: P33219 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 11883.17 |
構造登録者 | Prehna, G.,Zhang, G.,Gong, X.,Duszyk, M.,Okon, M.,Mcintosh, L.P.,Weiner, J.H.,Strynadka, N.C.J. (登録日: 2012-03-16, 公開日: 2012-06-13, 最終更新日: 2023-06-14) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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