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-基本情報
登録情報 | データベース: PDB / ID: 8hzq | ||||||
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タイトル | Bacillus subtilis SepF protein assembly (wild type) | ||||||
要素 | Cell division protein SepF | ||||||
キーワード | PROTEIN FIBRIL / Cell division / Assembly / Interact with Z-ring / membrane-binding protein | ||||||
機能・相同性 | : 機能・相同性情報 | ||||||
生物種 | Bacillus subtilis (枯草菌) | ||||||
手法 | 個体NMR / distance geometry | ||||||
データ登録者 | Liu, W. | ||||||
資金援助 | 中国, 1件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2024 タイトル: Molecular basis for curvature formation in SepF polymerization. 著者: Wenjing Liu / Chang Zhang / Huawei Zhang / Shaojie Ma / Jing Deng / Daping Wang / Ziwei Chang / Jun Yang / 要旨: The self-assembly of proteins into curved structures plays an important role in many cellular processes. One good example of this phenomenon is observed in the septum-forming protein (SepF), which ...The self-assembly of proteins into curved structures plays an important role in many cellular processes. One good example of this phenomenon is observed in the septum-forming protein (SepF), which forms polymerized structures with uniform curvatures. SepF is essential for regulating the thickness of the septum during bacteria cell division. In , SepF polymerization involves two distinct interfaces, the β-β and α-α interfaces, which define the assembly unit and contact interfaces, respectively. However, the mechanism of curvature formation in this step is not yet fully understood. In this study, we employed solid-state NMR (SSNMR) to compare the structures of cyclic wild-type SepF assemblies with linear assemblies resulting from a mutation of G137 on the β-β interface. Our results demonstrate that while the sequence differences arise from the internal assembly unit, the dramatic changes in the shape of the assemblies depend on the α-α interface between the units. We further provide atomic-level insights into how the angular variation of the α2 helix on the α-α interface affects the curvature of the assemblies, using a combination of SSNMR, cryo-electron microscopy, and simulation methods. Our findings shed light on the shape control of protein assemblies and emphasize the importance of interhelical contacts in retaining curvature. | ||||||
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 | 8hzq.cif.gz | 494 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb8hzq.ent.gz | 413.8 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 8hzq.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 | 8hzq_validation.pdf.gz | 391.9 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 8hzq_full_validation.pdf.gz | 440.9 KB | 表示 | |
XML形式データ | 8hzq_validation.xml.gz | 21.6 KB | 表示 | |
CIF形式データ | 8hzq_validation.cif.gz | 31.8 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/hz/8hzq ftp://data.pdbj.org/pub/pdb/validation_reports/hz/8hzq | HTTPS FTP |
-関連構造データ
関連構造データ | 8hztC 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 |
その他のデータベース |
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-リンク
-集合体
登録構造単位 |
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1 |
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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 8848.028 Da / 分子数: 2 / 由来タイプ: 組換発現 詳細: SepF was truncated to 57-151 of assembly state to accomplish the SSNMR experiments; sequence from 60 to 139 was chosen which included all the assigned section of chain A and B for dimer ...詳細: SepF was truncated to 57-151 of assembly state to accomplish the SSNMR experiments; sequence from 60 to 139 was chosen which included all the assigned section of chain A and B for dimer calculation during CS-Rosetta structure calculation 由来: (組換発現) Bacillus subtilis (枯草菌) / 遺伝子: sepF / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: A0A857HFW2 |
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-実験情報
-実験
実験 | 手法: 個体NMR | ||||||||||||||||||||||||||||||||||||
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NMR実験 |
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-試料調製
詳細 | タイプ: solid / 内容: 66 % 15N/13C SepF, ethanol/water 詳細: 15N/13C labeled SepF assembly 57-151 (wild type) for solid-state NMR (ssNMR) Label: 15N/13C / 溶媒系: ethanol/water |
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試料 | 濃度: 66 % / 構成要素: SepF / Isotopic labeling: 15N/13C |
試料状態 | イオン強度: 0 M / Label: 15N/13C / pH: 8.5 / 圧: 1 atm / 温度: 273 K |
-NMR測定
NMRスペクトロメーター | タイプ: Varian SepF Assembly 57 151 Wild type / 製造業者: Varian / モデル: SepF Assembly 57 151 Wild type / 磁場強度: 600 MHz / 詳細: with 3.2 BIOMAS probe |
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-解析
NMR software |
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精密化 | 手法: distance geometry / ソフトェア番号: 3 | ||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 20000 / 登録したコンフォーマーの数: 10 |