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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 9mu2 | ||||||
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タイトル | SaPI1 neck structure with DNA, tail completion protein, and tape measure protein | ||||||
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![]() | VIRUS LIKE PARTICLE / sapi / capsid / tail / phage | ||||||
機能・相同性 | ![]() | ||||||
生物種 | ![]() | ||||||
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: 3.54 Å | ||||||
![]() | Kizziah, J.L. / Dokland, T. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein. 著者: James L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland / ![]() 要旨: The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, ...The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs. #1: ジャーナル: bioRxiv / 年: 2024 タイトル: Structure of the bacteriophage 80α neck shows the interactions between DNA, tail completion protein and tape measure protein. 著者: James L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland / ![]() 要旨: Tailed bacteriophages with double-stranded DNA genomes (class ) play an important role in the evolution of bacterial pathogenicity, both as carriers of genes encoding virulence factors and as the ...Tailed bacteriophages with double-stranded DNA genomes (class ) play an important role in the evolution of bacterial pathogenicity, both as carriers of genes encoding virulence factors and as the main means of horizontal transfer of mobile genetic elements (MGEs) in many bacteria, such as . The pathogenicity islands (SaPIs), including SaPI1, are a type of MGEs are that carry a variable complement of genes encoding virulence factors. SaPI1 is mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI1 genome into virions made from structural proteins supplied by the helper. 80α and SaPI1 virions consist of an icosahedral head (capsid) connected via a unique vertex to a long, non-contractile tail. At one end of the tail, proteins associated with the baseplate recognize and bind to the host. At the other end, a connector or "neck" forms the interface between the tail and the head. The neck consists of several specialized proteins with specific roles in DNA packaging, phage assembly, and DNA ejection. Using cryo-electron microscopy and three-dimensional reconstruction, we have determined the high-resolution structure of the neck section of SaPI1 virions made in the presence of phage 80α, including the dodecameric portal (80α gene product (gp) 42) and head-tail-connector (gp49) proteins, the hexameric head-tail joining (gp50) and tail terminator (gp52) proteins, and the major tail protein (gp53) itself. We were also able to resolve the DNA, the tail completion protein (gp51) and the tape measure protein (gp56) inside the tail. This is the first detailed structural description of these features in a bacteriophage, providing insights into the assembly and infection process in this important group of MGEs and their helper bacteriophages. | ||||||
履歴 |
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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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ダウンロード
PDBx/mmCIF形式 | ![]() | 2.4 MB | 表示 | ![]() |
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PDB形式 | ![]() | 表示 | ![]() | |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
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 | ![]() 48617MC ![]() 9mu3C 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
-タンパク質 , 6種, 40分子 ABGHSTYZefklCIUagmDJVbhnEFKLWX...
#1: タンパク質 | 分子量: 12809.583 Da / 分子数: 12 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: S4V9M2 #2: タンパク質 | 分子量: 11815.448 Da / 分子数: 6 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: A0AA96SLM5 #3: タンパク質 | 分子量: 14730.251 Da / 分子数: 6 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: A4ZFB8 #4: タンパク質 | 分子量: 21551.746 Da / 分子数: 12 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: A4ZFB9 #5: タンパク質 | 分子量: 125891.977 Da / 分子数: 3 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: A4ZFC2 #6: タンパク質 | | 分子量: 13482.252 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: A0AA96SGB5 |
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-DNA鎖 , 2種, 2分子 QR
#7: DNA鎖 | 分子量: 13596138.000 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: GenBank: 148717842 |
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#8: DNA鎖 | 分子量: 13487673.000 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: GenBank: 148717842 |
-詳細
Has protein modification | N |
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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 |
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試料調製
構成要素 | 名称: Staphylococcus phage 80alpha / タイプ: VIRUS / Entity ID: all / 由来: NATURAL |
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由来(天然) | 生物種: ![]() |
ウイルスについての詳細 | 中空か: NO / エンベロープを持つか: NO / 単離: OTHER / タイプ: VIRUS-LIKE PARTICLE |
緩衝液 | pH: 7.8 |
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: TFS 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): 2000 nm / 最小 デフォーカス(公称値): 700 nm |
撮影 | 電子線照射量: 35.26 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 3.54 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 35724 / 対称性のタイプ: POINT |