SASDFR4: HP2042 form from Helicobacter pylori, N-terminal domain of syntax...

基本情報

• 登録情報: データベース: SASBDB / ID: SASDFR4

試料

HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:1WRT))

• HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (protein), Fusion protein1, Helicobacter pylori, Rattus norvegicus, Escherichia coli

• 生物種: Helicobacter pylori (ピロリ菌); Rattus norvegicus (ドブネズミ); Escherichia coli (大腸菌)
• 引用: ジャーナル: ACS Synth Biol / 年: 2019; タイトル: Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins.; 著者: Takaaki Miyamoto / Yugo Hayashi / Keito Yoshida / Hiroki Watanabe / Takayuki Uchihashi / Kento Yonezawa / Nobutaka Shimizu / Hironari Kamikubo / Shun Hirota / ; 要旨: Self-assembled protein nanostructures have gained interest, owing to their potential applications in biomaterials; however, successful design and construction of protein nanostructures are limited. Herein, we constructed fusion protein 1 by linking the C-terminus of a dimerization domain and the N-terminus of another dimerization domain with a three-helix bundle protein, where it self-assembled mainly into tetramers. By replacing the C-terminal dimerization domain of 1 with a trimerization domain (fusion protein 2), hexamers were mainly obtained. According to ab initio structural models reconstructed from the small-angle X-ray scattering data, the tetramer of 1 and hexamer of 2 adopted quadrangle and cage-like structures, respectively, although they were combinations of different conformations. High-speed atomic force microscopy observations indicated that the tetramer and hexamer exhibit conformational dynamics. These results show that the present method utilizing three-helix bundle-linked fusion proteins is useful in the construction of protein nanostructures.

登録者

• Hironari Kamikubo (Nara Institute of Science and Technology)

モデル

• モデル #2929: ; タイプ: mix / ダミー原子の半径: 1.90 A / カイ2乗値: 0.10 / P-value: 0.046149; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:1WRT)); 試料濃度: 2.30-8.30
• バッファ: 名称: 20 mM Tris-HCl 150 mM NaCl / pH: 8

要素 #1582

名称: Fusion protein1 / タイプ: protein
記述: HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli
分子量: 37.434 / 分子数: 4
由来: Helicobacter pylori, Rattus norvegicus, Escherichia coli
配列:

MGSSHHHHHH SSGLVPRGSH MRDYSELEIF EGNPLDKWND IIFHASKKAS KKELERLLEL LALCETFIEK EDLEEKFESF AKALRIDEEL QQKIESRKTD IVIQSMANIL SALFMDEFFE QVEEIRGFID KIAENVEEVK RKHSAILASP NPDEKTKEEL EELMSDIKKT ANKVRSKLKS IEQSIEQEEG LNRSSADLRI RKTQHSTLSR KFVEVMSEYN ATQSDYGSGS GRHQEWLRFV DLLKNAYQND LHLPLLNLML TPDEREALGT RVRIVEELLR GEMSQRELKN ELGAGIATIT RGSNSLKAAP VELRQWLEEV LLKSD

実験情報

• ビーム: 設備名称: Nara Institute of Science and Technology Rigaku Nano-Viewer; 地域: Ikoma / 国: Japan / 線源: X-ray in house / 波長: 0.15418 Å / スペクトロメータ・検出器間距離: 0.75 mm
• 検出器: 名称: Pilatus 200K / タイプ: Pilatus / Pixsize x: 172 mm

スキャン

タイトル: HP2042 form from Helicobacter pylori, N-terminal domain of syntaxin-1A from Rattus norvegicus, Trp repressor from Escherichia coli (Domain A (PDB:3MLI)-Linker (PDB:1BR0)-Domain B (PDB:1WRT))
測定日: 2016年12月8日 / 保管温度: 4 °C / セル温度: 20 °C / 照射時間: 60 sec. / フレーム数: 25 / 単位: 1/A /

	Min	Max
Q	0.0138	0.3003

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 220 /

	Min	Max
Q	0.01382	0.215586
P(R) point	1	220
R	0	200

結果

カーブのタイプ: extrapolated

	実験値	Standard	Standard error	Porod
分子量	177 kDa	177 kDa	4	237 kDa
体積	-	-	-	379 nm3

	P(R)	P(R) error	Guinier	Guinier error
前方散乱 I0	37.39	0.9	37.24	1.5
慣性半径, Rg	5.24 nm	2	5.11 nm	0.3

	Min	Max
D	-	20
Guinier point	1	10