+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 8eoj | ||||||
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タイトル | Microsomal triglyceride transfer protein | ||||||
要素 |
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キーワード | TRANSPORT PROTEIN / Microsomal triglyceride transfer protein / human liver / LIPID TRANSPORT / ISOMERASE | ||||||
機能・相同性 | 機能・相同性情報 plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / phosphatidylcholine transfer activity / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / phosphatidylethanolamine transfer activity / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing ...plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / phosphatidylcholine transfer activity / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / phosphatidylethanolamine transfer activity / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing / triglyceride transport / phospholipid transfer activity / procollagen-proline 4-dioxygenase activity / LDL remodeling / thiol oxidase activity / protein disulfide-isomerase / ceramide 1-phosphate transfer activity / very-low-density lipoprotein particle assembly / phospholipid transporter activity / endoplasmic reticulum chaperone complex / protein folding in endoplasmic reticulum / lipoprotein metabolic process / Collagen biosynthesis and modifying enzymes / Chylomicron assembly / interleukin-23-mediated signaling pathway / lipid transporter activity / phospholipid transport / cholesterol transfer activity / Interleukin-23 signaling / low-density lipoprotein particle remodeling / interleukin-12-mediated signaling pathway / cellular response to interleukin-7 / Interleukin-12 signaling / triglyceride metabolic process / lipoprotein transport / microvillus membrane / Insulin processing / protein disulfide isomerase activity / Detoxification of Reactive Oxygen Species / apolipoprotein binding / endoplasmic reticulum-Golgi intermediate compartment / protein-disulfide reductase activity / protein secretion / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of substrate adhesion-dependent cell spreading / response to endoplasmic reticulum stress / positive regulation of cell adhesion / cholesterol homeostasis / establishment of localization in cell / Post-translational protein phosphorylation / brush border membrane / Hedgehog ligand biogenesis / lipid metabolic process / response to calcium ion / circadian rhythm / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / integrin binding / melanosome / protein folding / lamellipodium / actin binding / cellular response to hypoxia / basolateral plasma membrane / vesicle / positive regulation of viral entry into host cell / cytoskeleton / receptor complex / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / focal adhesion / lipid binding / protein-containing complex binding / Golgi apparatus / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / extracellular exosome / extracellular region / cytosol 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
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: 3.07 Å | ||||||
データ登録者 | Zhang, Z. | ||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Cell Rep / 年: 2023 タイトル: High-resolution structural-omics of human liver enzymes. 著者: Chih-Chia Su / Meinan Lyu / Zhemin Zhang / Masaru Miyagi / Wei Huang / Derek J Taylor / Edward W Yu / 要旨: We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined ...We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined high-resolution structural information for ten unique human liver enzymes involved in diverse cellular processes. Notably, we determined the structure of the endoplasmic bifunctional protein H6PD, where the N- and C-terminal domains independently possess glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase enzymatic activity, respectively. We also obtained the structure of heterodimeric human GANAB, an ER glycoprotein quality-control machinery that contains a catalytic α subunit and a noncatalytic β subunit. In addition, we observed a decameric peroxidase, PRDX4, which directly contacts a disulfide isomerase-related protein, ERp46. Structural data suggest that several glycosylations, bound endogenous compounds, and ions associate with these human liver enzymes. These results highlight the importance of cryo-EM in facilitating the elucidation of human organ proteomics at the atomic level. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 8eoj.cif.gz | 244.7 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb8eoj.ent.gz | 191.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 8eoj.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 | 8eoj_validation.pdf.gz | 1.4 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 8eoj_full_validation.pdf.gz | 1.4 MB | 表示 | |
XML形式データ | 8eoj_validation.xml.gz | 48.6 KB | 表示 | |
CIF形式データ | 8eoj_validation.cif.gz | 71.6 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/eo/8eoj ftp://data.pdbj.org/pub/pdb/validation_reports/eo/8eoj | HTTPS FTP |
-関連構造データ
関連構造データ | 23426 28377MC 7uzmC 8ekwC 8ekyC 8em2C 8emrC 8emsC 8emtC 8eneC 8eorC 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 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
#1: タンパク質 | 分子量: 57190.137 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P07237, protein disulfide-isomerase |
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#2: タンパク質 | 分子量: 99474.102 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: P55157 |
-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: 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: Microsomal triglyceride transfer protein / タイプ: COMPLEX / Entity ID: all / 由来: NATURAL |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
緩衝液 | pH: 7.5 |
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 |
-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: 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): 81000 X / 最大 デフォーカス(公称値): 3291 nm / 最小 デフォーカス(公称値): 170 nm |
撮影 | 電子線照射量: 41.25 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / 分類: 精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
粒子像の選択 | 選択した粒子像数: 487553 | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.07 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 249877 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
精密化 | 交差検証法: NONE 立体化学のターゲット値: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 72.46 Å2 | ||||||||||||||||||||||||
拘束条件 |
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