7B5H
Cryo-EM structure of the contractile injection system base plate from Anabaena PCC7120
これはPDB形式変換不可エントリーです。
7B5H の概要
エントリーDOI | 10.2210/pdb7b5h/pdb |
関連するPDBエントリー | 7B5I |
EMDBエントリー | 12029 12030 12031 12032 12033 12034 |
分子名称 | All3314 protein, All3324 protein, All3325 protein, ... (11 entities in total) |
機能のキーワード | contractile tail, injection system, macromolecular machine, protein transport |
由来する生物種 | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) 詳細 |
タンパク質・核酸の鎖数 | 96 |
化学式量合計 | 6722331.56 |
構造登録者 | |
主引用文献 | Weiss, G.L.,Eisenstein, F.,Kieninger, A.K.,Xu, J.,Minas, H.A.,Gerber, M.,Feldmuller, M.,Maldener, I.,Forchhammer, K.,Pilhofer, M. Structure of a thylakoid-anchored contractile injection system in multicellular cyanobacteria. Nat Microbiol, 7:386-396, 2022 Cited by PubMed Abstract: Contractile injection systems (CISs) mediate cell-cell interactions by phage tail-like structures, using two distinct modes of action: extracellular CISs are released into the medium, while type 6 secretion systems (T6SSs) are attached to the cytoplasmic membrane and function upon cell-cell contact. Here, we characterized a CIS in the multicellular cyanobacterium Anabaena, with features distinct from extracellular CISs and T6SSs. Cryo-electron tomography of focused ion beam-milled cells revealed that CISs were anchored in thylakoid membrane stacks, facing the cell periphery. Single particle cryo-electron microscopy showed that this unique in situ localization was mediated by extensions of tail fibre and baseplate components. On stress, cyanobacteria induced the formation of ghost cells, presenting thylakoid-anchored CISs to the environment. Functional assays suggest that these CISs may mediate ghost cell formation and/or interactions of ghost cells with other organisms. Collectively, these data provide a framework for understanding the evolutionary re-engineering of CISs and potential roles of these CISs in cyanobacterial programmed cell death. PubMed: 35165386DOI: 10.1038/s41564-021-01055-y 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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