- PDB-4uv2: Structure of the curli transport lipoprotein CsgG in a non-lipida... -
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基本情報
登録情報
データベース: PDB / ID: 4uv2
タイトル
Structure of the curli transport lipoprotein CsgG in a non-lipidated, pre-pore conformation
要素
CURLI PRODUCTION TRANSPORT COMPONENT CSGG
キーワード
TRANSPORT PROTEIN / OUTER MEMBRANE PROTEIN
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
Curli production assembly/transport component CsgG / Curli production assembly/transport component CsgG / Prokaryotic membrane lipoprotein lipid attachment site profile. 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.
A: CURLI PRODUCTION TRANSPORT COMPONENT CSGG B: CURLI PRODUCTION TRANSPORT COMPONENT CSGG C: CURLI PRODUCTION TRANSPORT COMPONENT CSGG D: CURLI PRODUCTION TRANSPORT COMPONENT CSGG E: CURLI PRODUCTION TRANSPORT COMPONENT CSGG F: CURLI PRODUCTION TRANSPORT COMPONENT CSGG G: CURLI PRODUCTION TRANSPORT COMPONENT CSGG H: CURLI PRODUCTION TRANSPORT COMPONENT CSGG I: CURLI PRODUCTION TRANSPORT COMPONENT CSGG J: CURLI PRODUCTION TRANSPORT COMPONENT CSGG K: CURLI PRODUCTION TRANSPORT COMPONENT CSGG L: CURLI PRODUCTION TRANSPORT COMPONENT CSGG M: CURLI PRODUCTION TRANSPORT COMPONENT CSGG N: CURLI PRODUCTION TRANSPORT COMPONENT CSGG O: CURLI PRODUCTION TRANSPORT COMPONENT CSGG P: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
A: CURLI PRODUCTION TRANSPORT COMPONENT CSGG B: CURLI PRODUCTION TRANSPORT COMPONENT CSGG C: CURLI PRODUCTION TRANSPORT COMPONENT CSGG D: CURLI PRODUCTION TRANSPORT COMPONENT CSGG E: CURLI PRODUCTION TRANSPORT COMPONENT CSGG F: CURLI PRODUCTION TRANSPORT COMPONENT CSGG G: CURLI PRODUCTION TRANSPORT COMPONENT CSGG H: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
I: CURLI PRODUCTION TRANSPORT COMPONENT CSGG J: CURLI PRODUCTION TRANSPORT COMPONENT CSGG K: CURLI PRODUCTION TRANSPORT COMPONENT CSGG L: CURLI PRODUCTION TRANSPORT COMPONENT CSGG M: CURLI PRODUCTION TRANSPORT COMPONENT CSGG N: CURLI PRODUCTION TRANSPORT COMPONENT CSGG O: CURLI PRODUCTION TRANSPORT COMPONENT CSGG P: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
波長: 0.9795 Å / 相対比: 1
反射
解像度: 2.8→30 Å / Num. obs: 112419 / % possible obs: 98.7 % / Observed criterion σ(I): 2 / 冗長度: 11.2 % / Biso Wilson estimate: 46.8 Å2 / Rmerge(I) obs: 0.15 / Net I/σ(I): 9.82
反射 シェル
解像度: 2.8→2.9 Å / 冗長度: 7 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 2 / % possible all: 98.3
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解析
ソフトウェア
名称
バージョン
分類
PHENIX
(PHENIX.REFINE)
精密化
XDS
データ削減
XSCALE
データスケーリング
XSCALE
位相決定
精密化
構造決定の手法: 単波長異常分散 開始モデル: NONE 解像度: 2.8→29.765 Å / SU ML: 0.35 / σ(F): 2.12 / 位相誤差: 23.79 / 立体化学のターゲット値: MLHL 詳細: DISORDERED SIDECHAINS WERE MODELED STEREOCHEMICALLY AND ARE INDICATED BY A 0 OCCUPANCY
Rfactor
反射数
%反射
Rfree
0.2337
5620
5 %
Rwork
0.1881
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obs
0.1903
112369
98.98 %
溶媒の処理
減衰半径: 0.9 Å / VDWプローブ半径: 1.11 Å / 溶媒モデル: FLAT BULK SOLVENT MODEL