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-Structure paper
タイトル | Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex. |
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ジャーナル・号・ページ | Cell, Vol. 166, Issue 6, Page 1436-1444.e10, Year 2016 |
掲載日 | 2016年9月8日 |
著者 | Tiago R D Costa / Aravindan Ilangovan / Marta Ukleja / Adam Redzej / Joanne M Santini / Terry K Smith / Edward H Egelman / Gabriel Waksman / |
PubMed 要旨 | Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among ...Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among conjugative pili, the F "sex" pilus encoded by the F plasmid is the best functionally characterized, and it is also historically the most important, as the discovery of F-plasmid-mediated conjugation ushered in the era of molecular biology and genetics. Yet, its structure is unknown. Here, we present atomic models of two F family pili, the F and pED208 pili, generated from cryoelectron microscopy reconstructions at 5.0 and 3.6 Å resolution, respectively. These structures reveal that conjugative pili are assemblies of stoichiometric protein-phospholipid units. We further demonstrate that each pilus type binds preferentially to particular phospholipids. These structures provide the molecular basis for F pilus assembly and also shed light on the remarkable properties of conjugative pili in bacterial secretion and phage infection. |
リンク | Cell / PubMed:27610568 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.6 - 5.0 Å |
構造データ | EMDB-4042: Cryo-EM structure of the bacterial sex F pilus (pED208) |
化合物 | ChemComp-LHG: ChemComp-6V6: |
由来 |
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キーワード | PROTEIN FIBRIL / F-pilus Conjugation Type IV secretion system Phospholipid / Cell adhesion |