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基本情報
登録情報 | データベース: EMDB / ID: EMD-31400 | |||||||||||||||||||||
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タイトル | STRUCTURE OF PHOTOSYNTHETIC LH1-RC SUPER-COMPLEX OF RHODOBACTER SPHAEROIDES MONOMER | |||||||||||||||||||||
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機能・相同性 | ![]() organelle inner membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthesis, light reaction / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / membrane => GO:0016020 / metal ion binding / plasma membrane 類似検索 - 分子機能 | |||||||||||||||||||||
生物種 | ![]() ![]() ![]() | |||||||||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.94 Å | |||||||||||||||||||||
![]() | Tani K / Nagashima VP / Kanno R / Kawamura S / Kikuchi R / Ji X-C / Hall M / Yu L-J / Kimura Y / Madigan MT ...Tani K / Nagashima VP / Kanno R / Kawamura S / Kikuchi R / Ji X-C / Hall M / Yu L-J / Kimura Y / Madigan MT / Mizoguchi A / Humbel BM / Wang-Otomo Z-Y | |||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex. 著者: Kazutoshi Tani / Kenji V P Nagashima / Ryo Kanno / Saki Kawamura / Riku Kikuchi / Malgorzata Hall / Long-Jiang Yu / Yukihiro Kimura / Michael T Madigan / Akira Mizoguchi / Bruno M Humbel / ...著者: Kazutoshi Tani / Kenji V P Nagashima / Ryo Kanno / Saki Kawamura / Riku Kikuchi / Malgorzata Hall / Long-Jiang Yu / Yukihiro Kimura / Michael T Madigan / Akira Mizoguchi / Bruno M Humbel / Zheng-Yu Wang-Otomo / ![]() ![]() ![]() 要旨: Rhodobacter (Rba.) sphaeroides is the most widely used model organism in bacterial photosynthesis. The light-harvesting-reaction center (LH1-RC) core complex of this purple phototroph is ...Rhodobacter (Rba.) sphaeroides is the most widely used model organism in bacterial photosynthesis. The light-harvesting-reaction center (LH1-RC) core complex of this purple phototroph is characterized by the co-existence of monomeric and dimeric forms, the presence of the protein PufX, and approximately two carotenoids per LH1 αβ-polypeptides. Despite many efforts, structures of the Rba. sphaeroides LH1-RC have not been obtained at high resolutions. Here we report a cryo-EM structure of the monomeric LH1-RC from Rba. sphaeroides strain IL106 at 2.9 Å resolution. The LH1 complex forms a C-shaped structure composed of 14 αβ-polypeptides around the RC with a large ring opening. From the cryo-EM density map, a previously unrecognized integral membrane protein, referred to as protein-U, was identified. Protein-U has a U-shaped conformation near the LH1-ring opening and was annotated as a hypothetical protein in the Rba. sphaeroides genome. Deletion of protein-U resulted in a mutant strain that expressed a much-reduced amount of the dimeric LH1-RC, indicating an important role for protein-U in dimerization of the LH1-RC complex. PufX was located opposite protein-U on the LH1-ring opening, and both its position and conformation differed from that of previous reports of dimeric LH1-RC structures obtained at low-resolution. Twenty-six molecules of the carotenoid spheroidene arranged in two distinct configurations were resolved in the Rba. sphaeroides LH1 and were positioned within the complex to block its channels. Our findings offer an exciting new view of the core photocomplex of Rba. sphaeroides and the connections between structure and function in bacterial photocomplexes in general. | |||||||||||||||||||||
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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画像 | ![]() | 187.2 KB | ||
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文書・詳細版 | ![]() | 577 KB | 表示 | |
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CIF形式データ | ![]() | 14.9 KB | 表示 | |
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マップ
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ボクセルのサイズ | X=Y=Z: 1.094 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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試料の構成要素
+全体 : Photosynthetic LH1-RC complex from the purple phototrophic bacter...
+超分子 #1: Photosynthetic LH1-RC complex from the purple phototrophic bacter...
+分子 #1: Photosynthetic reaction center L subunit
+分子 #2: Reaction center protein M chain
+分子 #3: Reaction center protein H chain
+分子 #4: Light-harvesting protein B-875 alpha chain
+分子 #5: Antenna pigment protein beta chain
+分子 #6: Light-harvesting protein B-875 alpha chain
+分子 #7: PufX
+分子 #8: protein-U
+分子 #9: BACTERIOCHLOROPHYLL A
+分子 #10: BACTERIOPHEOPHYTIN A
+分子 #11: UBIQUINONE-10
+分子 #12: (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-...
+分子 #13: LAURYL DIMETHYLAMINE-N-OXIDE
+分子 #14: FE (III) ION
+分子 #15: SPHEROIDENE
+分子 #16: DODECYL-BETA-D-MALTOSIDE
+分子 #17: CARDIOLIPIN
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
濃度 | 3.0 mg/mL |
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緩衝液 | pH: 8 |
グリッド | 材質: MOLYBDENUM |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 80 % / チャンバー内温度: 277 K / 装置: LEICA EM GP |
詳細 | This sample was monodisperse. |
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電子顕微鏡法
顕微鏡 | FEI TALOS ARCTICA |
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撮影 | フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 検出モード: COUNTING / 平均露光時間: 1.275 sec. / 平均電子線量: 42.0 e/Å2 |
電子線 | 加速電圧: 200 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Talos Arctica / 画像提供: FEI Company |