6MRU
13-meric ClyA pore complex
6MRU の概要
エントリーDOI | 10.2210/pdb6mru/pdb |
EMDBエントリー | 9213 |
分子名称 | Hemolysin E, chromosomal (1 entity in total) |
機能のキーワード | pore-forming toxin, membrane protein, toxin |
由来する生物種 | Escherichia coli (strain K12) |
タンパク質・核酸の鎖数 | 13 |
化学式量合計 | 469713.61 |
構造登録者 | Peng, W.,de Souza Santos, M.,Li, Y.,Tomchick, D.R.,Orth, K. (登録日: 2018-10-15, 公開日: 2019-05-15, 最終更新日: 2024-03-13) |
主引用文献 | Peng, W.,de Souza Santos, M.,Li, Y.,Tomchick, D.R.,Orth, K. High-resolution cryo-EM structures of the E. coli hemolysin ClyA oligomers. Plos One, 14:e0213423-e0213423, 2019 Cited by PubMed Abstract: Pore-forming proteins (PFPs) represent a functionally important protein family, that are found in organisms from viruses to humans. As a major branch of PFPs, bacteria pore-forming toxins (PFTs) permeabilize membranes and usually cause the death of target cells. E. coli hemolysin ClyA is the first member with the pore complex structure solved among α-PFTs, employing α-helices as transmembrane elements. ClyA is proposed to form pores composed of various numbers of protomers. With high-resolution cryo-EM structures, we observe that ClyA pore complexes can exist as newly confirmed oligomers of a tridecamer and a tetradecamer, at estimated resolutions of 3.2 Å and 4.3 Å, respectively. The 2.8 Å cryo-EM structure of a dodecamer dramatically improves the existing structural model. Structural analysis indicates that protomers from distinct oligomers resemble each other and neighboring protomers adopt a conserved interaction mode. We also show a stabilized intermediate state of ClyA during the transition process from soluble monomers to pore complexes. Unexpectedly, even without the formation of mature pore complexes, ClyA can permeabilize membranes and allow leakage of particles less than ~400 Daltons. In addition, we are the first to show that ClyA forms pore complexes in the presence of cholesterol within artificial liposomes. These findings provide new mechanistic insights into the dynamic process of pore assembly for the prototypical α-PFT ClyA. PubMed: 31048915DOI: 10.1371/journal.pone.0213423 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
構造検証レポート
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