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6MRU

13-meric ClyA pore complex

6MRU の概要
エントリーDOI10.2210/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: 31048915
DOI: 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
Validation report summary of 6mru
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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