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-Structure paper
タイトル | Structure and transformation of bacteriophage A511 baseplate and tail upon infection of cells. |
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ジャーナル・号・ページ | EMBO J, Vol. 38, Issue 3, Year 2019 |
掲載日 | 2019年2月1日 |
著者 | Ricardo C Guerrero-Ferreira / Mario Hupfeld / Sergey Nazarov / Nicholas Mi Taylor / Mikhail M Shneider / Jagan M Obbineni / Martin J Loessner / Takashi Ishikawa / Jochen Klumpp / Petr G Leiman / |
PubMed 要旨 | Contractile injection systems (bacteriophage tails, type VI secretions system, R-type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and ...Contractile injection systems (bacteriophage tails, type VI secretions system, R-type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and eukaryotic cells. Among contractile injection systems, bacteriophages that infect Gram-positive bacteria represent the least understood members. Here, we describe the structure of bacteriophage A511 tail in its pre- and post-host attachment states (extended and contracted, respectively) using cryo-electron microscopy, cryo-electron tomography, and X-ray crystallography. We show that the structure of the tube-baseplate complex of A511 is similar to that of phage T4, but the A511 baseplate is decorated with different receptor-binding proteins, which undergo a large structural transformation upon host attachment and switch the symmetry of the baseplate-tail fiber assembly from threefold to sixfold. For the first time under native conditions, we show that contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a domino-like motion. |
リンク | EMBO J / PubMed:30606715 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.38 - 16.0 Å |
構造データ | EMDB-7559: EMDB-7560: EMDB-7561: PDB-6hhk: |
化合物 | ChemComp-CL: ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN (ウイルスタンパク質) / bacteriophage baseplate protein |