+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 4a0w | ||||||
---|---|---|---|---|---|---|---|
タイトル | model built against symmetry-free cryo-EM map of TRiC-ADP-AlFx | ||||||
要素 | T-COMPLEX PROTEIN 1 SUBUNIT BETA | ||||||
キーワード | CHAPERONE / CHAPERONIN / PROTEIN FOLDING | ||||||
機能・相同性 | 機能・相同性情報 Association of TriC/CCT with target proteins during biosynthesis / RHOBTB2 GTPase cycle / RHOBTB1 GTPase cycle / chaperonin-containing T-complex / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Neutrophil degranulation / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding 類似検索 - 分子機能 | ||||||
生物種 | BOS TAURUS (ウシ) | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 13.9 Å | ||||||
データ登録者 | Cong, Y. / Schroder, G.F. / Meyer, A.S. / Jakana, J. / Ma, B. / Dougherty, M.T. / Schmid, M.F. / Reissmann, S. / Levitt, M. / Ludtke, S.L. ...Cong, Y. / Schroder, G.F. / Meyer, A.S. / Jakana, J. / Ma, B. / Dougherty, M.T. / Schmid, M.F. / Reissmann, S. / Levitt, M. / Ludtke, S.L. / Frydman, J. / Chiu, W. | ||||||
引用 | ジャーナル: EMBO J / 年: 2012 タイトル: Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. 著者: Yao Cong / Gunnar F Schröder / Anne S Meyer / Joanita Jakana / Boxue Ma / Matthew T Dougherty / Michael F Schmid / Stefanie Reissmann / Michael Levitt / Steven L Ludtke / Judith Frydman / Wah Chiu / 要旨: The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered ...The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar subunits arranged in two stacked rings. Substrate folding inside the central chamber is triggered by ATP hydrolysis. We present five cryo-EM structures of TRiC in apo and nucleotide-induced states without imposing symmetry during the 3D reconstruction. These structures reveal the intra- and inter-ring subunit interaction pattern changes during the ATPase cycle. In the apo state, the subunit arrangement in each ring is highly asymmetric, whereas all nucleotide-containing states tend to be more symmetrical. We identify and structurally characterize an one-ring closed intermediate induced by ATP hydrolysis wherein the closed TRiC ring exhibits an observable chamber expansion. This likely represents the physiological substrate folding state. Our structural results suggest mechanisms for inter-ring-negative cooperativity, intra-ring-positive cooperativity, and protein-folding chamber closure of TRiC. Intriguingly, these mechanisms are different from other group I and II chaperonins despite their similar architecture. | ||||||
履歴 |
|
-構造の表示
ムービー |
ムービービューア |
---|---|
構造ビューア | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 4a0w.cif.gz | 1.2 MB | 表示 | PDBx/mmCIF形式 |
---|---|---|---|---|
PDB形式 | pdb4a0w.ent.gz | 1 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 4a0w.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 4a0w_validation.pdf.gz | 946.4 KB | 表示 | wwPDB検証レポート |
---|---|---|---|---|
文書・詳細版 | 4a0w_full_validation.pdf.gz | 1.3 MB | 表示 | |
XML形式データ | 4a0w_validation.xml.gz | 235.1 KB | 表示 | |
CIF形式データ | 4a0w_validation.cif.gz | 356.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/a0/4a0w ftp://data.pdbj.org/pub/pdb/validation_reports/a0/4a0w | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
|
---|---|
1 |
|
-要素
#1: タンパク質 | 分子量: 55107.234 Da / 分子数: 16 / 由来タイプ: 天然 / 由来: (天然) BOS TAURUS (ウシ) / 器官: TESTES / 参照: UniProt: Q3ZBH0 |
---|
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
---|---|
EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-試料調製
構成要素 | 名称: BOVINE TRIC IN THE AMP- PNP STATE / タイプ: COMPLEX |
---|---|
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | 詳細: HOLEY CARBON |
急速凍結 | 装置: FEI VITROBOT MARK I / 凍結剤: ETHANE |
-電子顕微鏡撮影
顕微鏡 | モデル: JEOL 3200FSC |
---|---|
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 50000 X / 最大 デフォーカス(公称値): 3000 nm / 最小 デフォーカス(公称値): 1200 nm / Cs: 4.1 mm |
試料ホルダ | 温度: 101 K |
撮影 | 電子線照射量: 18 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM |
画像スキャン | デジタル画像の数: 300 |
-解析
EMソフトウェア | 名称: EMAN / バージョン: 1.8 / カテゴリ: 3次元再構成 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF補正 | 詳細: EACH MICROGRAPH | ||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||
3次元再構成 | 手法: PROJECTION MATCHING / 解像度: 13.9 Å / 粒子像の数: 16495 / ピクセルサイズ(公称値): 2.4 Å / ピクセルサイズ(実測値): 2.4 Å 詳細: OUR MODELS DO NOT INCLUDE SOME REGIONS OF THE APICAL DOMAIN IN SEVERAL SUBUNITS, BECAUSE THE MAP IN THOSE REGIONS WAS NOT VERY WELL RESOLVED DUE TO THE DYNAMIC NATURE OF THOSE SUBUNITS. WE ...詳細: OUR MODELS DO NOT INCLUDE SOME REGIONS OF THE APICAL DOMAIN IN SEVERAL SUBUNITS, BECAUSE THE MAP IN THOSE REGIONS WAS NOT VERY WELL RESOLVED DUE TO THE DYNAMIC NATURE OF THOSE SUBUNITS. WE FITTED THE MODEL WITH THE OCCUPANCY REFINEMENT FEATURE IN DIREX. THIS BASICALLY DETERMINES WHETHER THERE IS SUFFICIENT DENSITY FOR EACH RESIDUE OR IF THERE IS REDUCED OR MISSING DENSITY. THE OCCUPANCY IS VALUE BETWEEN 0 AND 1. WE WROTE THIS VALUE INTO THE B-FACTOR COLUMN AS 100X(1-OCCUPANCY). THIS RESEMBLES A B-FACTOR BUT IS NOT EXACTLY THE SAME. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-1962. (DEPOSITION ID: 10237). 対称性のタイプ: POINT | ||||||||||||
精密化 | 最高解像度: 13.9 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 13.9 Å
|