+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6ql5 | ||||||
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タイトル | Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom | ||||||
要素 |
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キーワード | TRANSFERASE / Fatty acid synthase / Acyl carrier protein / Ketosynthase / Ketoreductase / Enoyl reductase / Dehydratase / Malonyl/palmitoyl transferase / Acetyl transferase / Phosphopantetheine transferase | ||||||
機能・相同性 | 機能・相同性情報 fatty-acyl-CoA synthase system / fatty acid synthase complex / fatty-acyl-CoA synthase activity / [acyl-carrier-protein] S-acetyltransferase / palmitoyltransferase activity / [acyl-carrier-protein] S-acetyltransferase activity / : / oleoyl-[acyl-carrier-protein] hydrolase / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / fatty acyl-[ACP] hydrolase activity ...fatty-acyl-CoA synthase system / fatty acid synthase complex / fatty-acyl-CoA synthase activity / [acyl-carrier-protein] S-acetyltransferase / palmitoyltransferase activity / [acyl-carrier-protein] S-acetyltransferase activity / : / oleoyl-[acyl-carrier-protein] hydrolase / (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity / fatty acyl-[ACP] hydrolase activity / proteasome regulatory particle assembly / holo-[acyl-carrier-protein] synthase activity / enoyl-[acyl-carrier-protein] reductase (NADPH) activity / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / enoyl-[acyl-carrier-protein] reductase (NADH) / long-chain fatty acid biosynthetic process / fatty acid synthase activity / enoyl-[acyl-carrier-protein] reductase (NADH) activity / 3-oxoacyl-[acyl-carrier-protein] synthase activity / lipid droplet / fatty acid biosynthetic process / protein-macromolecule adaptor activity / magnesium ion binding / mitochondrion / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | Saccharomyces cerevisiae (パン酵母) | ||||||
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: 2.8 Å | ||||||
データ登録者 | Singh, K. / Graf, B. / Linden, A. / Sautner, V. / Urlaub, H. / Tittmann, K. / Stark, H. / Chari, A. | ||||||
資金援助 | ドイツ, 1件
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引用 | ジャーナル: Cell / 年: 2020 タイトル: Discovery of a Regulatory Subunit of the Yeast Fatty Acid Synthase. 著者: Kashish Singh / Benjamin Graf / Andreas Linden / Viktor Sautner / Henning Urlaub / Kai Tittmann / Holger Stark / Ashwin Chari / 要旨: Fatty acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid ...Fatty acid synthases (FASs) are central to metabolism but are also of biotechnological interest for the production of fine chemicals and biofuels from renewable resources. During fatty acid synthesis, the growing fatty acid chain is thought to be shuttled by the dynamic acyl carrier protein domain to several enzyme active sites. Here, we report the discovery of a γ subunit of the 2.6 megadalton α-βS. cerevisiae FAS, which is shown by high-resolution structures to stabilize a rotated FAS conformation and rearrange ACP domains from equatorial to axial positions. The γ subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The γ subunit delineates the functional compartment within FAS. As a scaffold, it may be exploited to incorporate natural and designed enzymatic activities that are not present in natural FAS. | ||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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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 | 6ql5.cif.gz | 4.3 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6ql5.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 6ql5.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 | 6ql5_validation.pdf.gz | 2 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6ql5_full_validation.pdf.gz | 2.3 MB | 表示 | |
XML形式データ | 6ql5_validation.xml.gz | 524.2 KB | 表示 | |
CIF形式データ | 6ql5_validation.cif.gz | 834.7 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ql/6ql5 ftp://data.pdbj.org/pub/pdb/validation_reports/ql/6ql5 | HTTPS FTP |
-関連構造データ
関連構造データ | 4577MC 4578C 6ql6C 6ql7C 6ql9C 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 | |
電子顕微鏡画像生データ | EMPIAR-10454 (タイトル: Saccharomyces cerevisiae fatty acid synthase complex with bound gamma subunit Data size: 329.3 Data #1: Aligned and doseweighted micrographs of yeast fatty acid synthase with bound gamma subunit [micrographs - single frame] Data #2: Stack of Polished particles (in relion) used for final reconstruction [picked particles - single frame - processed]) |
-リンク
-集合体
登録構造単位 |
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-要素
#1: タンパク質 | 分子量: 207184.422 Da / 分子数: 6 / 由来タイプ: 天然 / 由来: (天然) Saccharomyces cerevisiae (パン酵母) 参照: UniProt: P19097, fatty-acyl-CoA synthase system, 3-oxoacyl-[acyl-carrier-protein] reductase, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: タンパク質 | 分子量: 227785.141 Da / 分子数: 6 / 由来タイプ: 天然 / 由来: (天然) Saccharomyces cerevisiae (パン酵母) 参照: UniProt: P07149, fatty-acyl-CoA synthase system, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, enoyl-[acyl-carrier-protein] reductase (NADH), [acyl-carrier-protein] S-acetyltransferase, ...参照: UniProt: P07149, fatty-acyl-CoA synthase system, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, enoyl-[acyl-carrier-protein] reductase (NADH), [acyl-carrier-protein] S-acetyltransferase, [acyl-carrier-protein] S-malonyltransferase, oleoyl-[acyl-carrier-protein] hydrolase #3: タンパク質 | 分子量: 16558.117 Da / 分子数: 6 / 由来タイプ: 天然 / 由来: (天然) Saccharomyces cerevisiae (パン酵母) / 参照: UniProt: Q12513 #4: 化合物 | ChemComp-PNS / #5: 化合物 | ChemComp-FMN / |
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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: 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: Fatty acid synthase holoenzyme complex at 2.8 angstrom resolution タイプ: COMPLEX / Entity ID: #1-#3 / 由来: NATURAL | ||||||||||||||||||||
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分子量 | 値: 2.6 MDa / 実験値: YES | ||||||||||||||||||||
由来(天然) | 生物種: Saccharomyces cerevisiae (パン酵母) 株: BJ2168 (MATa prc1-407 prb1-1122 pep4-3 leu2 trp1 ura3-52 gal2 tma17::kanMX) | ||||||||||||||||||||
緩衝液 | pH: 6.5 | ||||||||||||||||||||
緩衝液成分 |
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試料 | 濃度: 0.5 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 278 K |
-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): 132000 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): 1000 nm / Cs: 2.7 mm / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 電子線照射量: 48 e/Å2 / 検出モード: INTEGRATING フィルム・検出器のモデル: FEI FALCON III (4k x 4k) 実像数: 5441 |
-解析
EMソフトウェア |
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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: 856940 | ||||||||||||||||||||||||
対称性 | 点対称性: D3 (2回x3回 2面回転対称) | ||||||||||||||||||||||||
3次元再構成 | 解像度: 2.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 110597 / 対称性のタイプ: POINT |