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基本情報
登録情報 | データベース: PDB / ID: 8eff | ||||||
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タイトル | CryoEM of the soluble OPA1 tetramer from the GDP-AlFx bound helical assembly on a lipid membrane | ||||||
![]() | Dynamin-like 120 kDa protein, form S1 | ||||||
![]() | LIPID BINDING PROTEIN / GTPase / Dynamin-family protein / mitochondrial fusion protein / mitochondria / Optic Atrophy | ||||||
機能・相同性 | ![]() Regulation of Apoptosis / mitochondrial inner membrane fusion / membrane tubulation / GTPase-dependent fusogenic activity / membrane bending activity / inner mitochondrial membrane organization / dynamin GTPase / cristae formation / mitochondrial genome maintenance / phosphatidic acid binding ...Regulation of Apoptosis / mitochondrial inner membrane fusion / membrane tubulation / GTPase-dependent fusogenic activity / membrane bending activity / inner mitochondrial membrane organization / dynamin GTPase / cristae formation / mitochondrial genome maintenance / phosphatidic acid binding / mitochondrial fission / cardiolipin binding / positive regulation of T-helper 17 cell lineage commitment / GTP metabolic process / mitochondrial fusion / axonal transport of mitochondrion / negative regulation of release of cytochrome c from mitochondria / mitochondrial crista / positive regulation of interleukin-17 production / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / axon cytoplasm / visual perception / mitochondrion organization / Mitochondrial protein degradation / neural tube closure / mitochondrial membrane / cellular senescence / mitochondrial intermembrane space / protein complex oligomerization / microtubule binding / mitochondrial outer membrane / microtubule / mitochondrial inner membrane / GTPase activity / dendrite / negative regulation of apoptotic process / GTP binding / apoptotic process / magnesium ion binding / mitochondrion / nucleoplasm / membrane / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 5.48 Å | ||||||
![]() | Nyenhuis, S.B. / Wu, X. / Stanton, A.E. / Strub, M.P. / Yim, Y.I. / Canagarajah, B. / Hinshaw, J.E. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: OPA1 helical structures give perspective to mitochondrial dysfunction. 著者: Sarah B Nyenhuis / Xufeng Wu / Marie-Paule Strub / Yang-In Yim / Abigail E Stanton / Valentina Baena / Zulfeqhar A Syed / Bertram Canagarajah / John A Hammer / Jenny E Hinshaw / ![]() 要旨: Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of cases are caused by mutations of the gene that encodes optic atrophy protein 1 (OPA1), a protein that has ...Dominant optic atrophy is one of the leading causes of childhood blindness. Around 60-80% of cases are caused by mutations of the gene that encodes optic atrophy protein 1 (OPA1), a protein that has a key role in inner mitochondrial membrane fusion and remodelling of cristae and is crucial for the dynamic organization and regulation of mitochondria. Mutations in OPA1 result in the dysregulation of the GTPase-mediated fusion process of the mitochondrial inner and outer membranes. Here we used cryo-electron microscopy methods to solve helical structures of OPA1 assembled on lipid membrane tubes, in the presence and absence of nucleotide. These helical assemblies organize into densely packed protein rungs with minimal inter-rung connectivity, and exhibit nucleotide-dependent dimerization of the GTPase domains-a hallmark of the dynamin superfamily of proteins. OPA1 also contains several unique secondary structures in the paddle domain that strengthen its membrane association, including membrane-inserting helices. The structural features identified in this study shed light on the effects of pathogenic point mutations on protein folding, inter-protein assembly and membrane interactions. Furthermore, mutations that disrupt the assembly interfaces and membrane binding of OPA1 cause mitochondrial fragmentation in cell-based assays, providing evidence of the biological relevance of these interactions. | ||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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PDBx/mmCIF形式 | ![]() | 1 MB | 表示 | ![]() |
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PDB形式 | ![]() | 883.1 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
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アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
関連構造データ | ![]() 28063MC ![]() 8eewC ![]() 8ef7C ![]() 8efrC ![]() 8efsC ![]() 8eftC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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リンク
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集合体
登録構造単位 | ![]()
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要素
#1: タンパク質 | 分子量: 89262.516 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #2: 化合物 | ChemComp-GDP / #3: 化合物 | ChemComp-ALF / #4: 化合物 | ChemComp-MG / #5: 化合物 | ChemComp-K / 研究の焦点であるリガンドがあるか | Y | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: HELICAL ARRAY / 3次元再構成法: らせん対称体再構成法 |
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試料調製
構成要素 | 名称: cryoEM of the soluble OPA1 tetramer from the GDP-AlFx bound helical assembly on a lipid membrane タイプ: COMPLEX / Entity ID: #1 / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 7.2 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2400 nm / 最小 デフォーカス(公称値): 300 nm |
撮影 | 電子線照射量: 60 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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解析
EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
らせん対称 | 回転角度/サブユニット: 37.439 ° / 軸方向距離/サブユニット: 12.933 Å / らせん対称軸の対称性: C1 | |||||||||
3次元再構成 | 解像度: 5.48 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 598503 / 対称性のタイプ: HELICAL | |||||||||
原子モデル構築 | プロトコル: FLEXIBLE FIT / 空間: REAL | |||||||||
原子モデル構築 | PDB-ID: 6JTG |