+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 7bgl | |||||||||||||||
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タイトル | Salmonella LP ring 26 mer refined in C26 map | |||||||||||||||
要素 |
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キーワード | MEMBRANE PROTEIN / bacterial flagellum LP ring salmonella | |||||||||||||||
機能・相同性 | 機能・相同性情報 bacterial-type flagellum basal body, distal rod, L ring / bacterial-type flagellum basal body, distal rod, P ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / cell outer membrane / outer membrane-bounded periplasmic space / structural molecule activity 類似検索 - 分子機能 | |||||||||||||||
生物種 | Salmonella typhimurium (サルモネラ菌) | |||||||||||||||
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: 2.2 Å | |||||||||||||||
データ登録者 | Johnson, S. / Furlong, E. / Lea, S.M. | |||||||||||||||
資金援助 | 英国, 4件
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引用 | ジャーナル: Nat Microbiol / 年: 2021 タイトル: Molecular structure of the intact bacterial flagellar basal body. 著者: Steven Johnson / Emily J Furlong / Justin C Deme / Ashley L Nord / Joseph J E Caesar / Fabienne F V Chevance / Richard M Berry / Kelly T Hughes / Susan M Lea / 要旨: The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the ...The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the inner membrane to the micrometre-long flagellar filament that powers bacterial swimming in viscous fluids. Here, we present structures of the intact Salmonella flagellar basal body, encompassing the inner membrane rotor, drive shaft and outer-membrane bushing, solved using cryo-electron microscopy to resolutions of 2.2-3.7 Å. The structures reveal molecular details of how 173 protein molecules of 13 different types assemble into a complex spanning two membranes and a cell wall. The helical drive shaft at one end is intricately interwoven with the rotor component with both the export gate complex and the proximal rod forming interactions with the MS-ring. At the other end, the drive shaft distal rod passes through the LP-ring bushing complex, which functions as a molecular bearing anchored in the outer membrane through interactions with the lipopolysaccharide. The in situ structure of a protein complex capping the drive shaft provides molecular insights into the assembly process of this molecular machine. | |||||||||||||||
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 | 7bgl.cif.gz | 2.7 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7bgl.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 7bgl.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 | 7bgl_validation.pdf.gz | 4.4 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7bgl_full_validation.pdf.gz | 4.8 MB | 表示 | |
XML形式データ | 7bgl_validation.xml.gz | 437.1 KB | 表示 | |
CIF形式データ | 7bgl_validation.cif.gz | 548.8 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/bg/7bgl ftp://data.pdbj.org/pub/pdb/validation_reports/bg/7bgl | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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非結晶学的対称性 (NCS) | NCSドメイン:
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