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2LRD

The solution structure of the monomeric Acanthaporin

2KU8」から置き換えられました
2LRD の概要
エントリーDOI10.2210/pdb2lrd/pdb
関連するPDBエントリー2LRE
NMR情報BMRB: 18357
分子名称Acanthaporin (1 entity in total)
機能のキーワードpore-forming toxin, alpha helix, antimicrobial protein
由来する生物種Acanthamoeba culbertsoni
タンパク質・核酸の鎖数1
化学式量合計6001.23
構造登録者
主引用文献Michalek, M.,Sonnichsen, F.D.,Wechselberger, R.,Dingley, A.J.,Hung, C.W.,Kopp, A.,Wienk, H.,Simanski, M.,Herbst, R.,Lorenzen, I.,Marciano-Cabral, F.,Gelhaus, C.,Gutsmann, T.,Tholey, A.,Grotzinger, J.,Leippe, M.
Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.
Nat.Chem.Biol., 9:37-42, 2013
Cited by
PubMed Abstract: Human pathogens often produce soluble protein toxins that generate pores inside membranes, resulting in the death of target cells and tissue damage. In pathogenic amoebae, this has been exemplified with amoebapores of the enteric protozoan parasite Entamoeba histolytica. Here we characterize acanthaporin, to our knowledge the first pore-forming toxin to be described from acanthamoebae, which are free-living, bacteria-feeding, unicellular organisms that are opportunistic pathogens of increasing importance and cause severe and often fatal diseases. We isolated acanthaporin from extracts of virulent Acanthamoeba culbertsoni by tracking its pore-forming activity, molecularly cloned the gene of its precursor and recombinantly expressed the mature protein in bacteria. Acanthaporin was cytotoxic for human neuronal cells and exerted antimicrobial activity against a variety of bacterial strains by permeabilizing their membranes. The tertiary structures of acanthaporin's active monomeric form and inactive dimeric form, both solved by NMR spectroscopy, revealed a currently unknown protein fold and a pH-dependent trigger mechanism of activation.
PubMed: 23143413
DOI: 10.1038/nchembio.1116
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lrd
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2024-10-30に公開中

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