- PDB-4uv3: Structure of the curli transport lipoprotein CsgG in its membrane... -
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基本情報
登録情報
データベース: PDB / ID: 4uv3
タイトル
Structure of the curli transport lipoprotein CsgG in its membrane- bound conformation
要素
CURLI PRODUCTION ASSEMBLY/TRANSPORT COMPONENT CSGG
キーワード
TRANSPORT PROTEIN / CSGG / CURLI TRANSPORTER / OUTER MEMBRANE LIPOPROTEIN / AMYLOID
機能・相同性
機能・相同性情報
curli secretion complex / curli assembly / protein secretion by the type VIII secretion system / protein transmembrane transport / single-species biofilm formation / cell outer membrane / outer membrane-bounded periplasmic space / identical protein binding / plasma membrane 類似検索 - 分子機能
ABC-type transport auxiliary lipoprotein component / Curli production assembly/transport component CsgG / Curli production assembly/transport component CsgG / Prokaryotic membrane lipoprotein lipid attachment site profile. / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta 類似検索 - ドメイン・相同性
Curli production assembly/transport component CsgG 類似検索 - 構成要素
ジャーナル: Nature / 年: 2014 タイトル: Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. 著者: Parveen Goyal / Petya V Krasteva / Nani Van Gerven / Francesca Gubellini / Imke Van den Broeck / Anastassia Troupiotis-Tsaïlaki / Wim Jonckheere / Gérard Péhau-Arnaudet / Jerome S Pinkner ...著者: Parveen Goyal / Petya V Krasteva / Nani Van Gerven / Francesca Gubellini / Imke Van den Broeck / Anastassia Troupiotis-Tsaïlaki / Wim Jonckheere / Gérard Péhau-Arnaudet / Jerome S Pinkner / Matthew R Chapman / Scott J Hultgren / Stefan Howorka / Rémi Fronzes / Han Remaut / 要旨: Curli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the α ...Curli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the α and γ classes). They provide a fitness advantage in pathogenic strains and induce a strong pro-inflammatory response during bacteraemia. Curli formation requires a dedicated protein secretion machinery comprising the outer membrane lipoprotein CsgG and two soluble accessory proteins, CsgE and CsgF. Here we report the X-ray structure of Escherichia coli CsgG in a non-lipidated, soluble form as well as in its native membrane-extracted conformation. CsgG forms an oligomeric transport complex composed of nine anticodon-binding-domain-like units that give rise to a 36-stranded β-barrel that traverses the bilayer and is connected to a cage-like vestibule in the periplasm. The transmembrane and periplasmic domains are separated by a 0.9-nm channel constriction composed of three stacked concentric phenylalanine, asparagine and tyrosine rings that may guide the extended polypeptide substrate through the secretion pore. The specificity factor CsgE forms a nonameric adaptor that binds and closes off the periplasmic face of the secretion channel, creating a 24,000 Å(3) pre-constriction chamber. Our structural, functional and electrophysiological analyses imply that CsgG is an ungated, non-selective protein secretion channel that is expected to employ a diffusion-based, entropy-driven transport mechanism.
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.