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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: 1mhs | ||||||
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タイトル | Model of Neurospora crassa proton ATPase | ||||||
![]() | Plasma Membrane ATPase | ||||||
![]() | MEMBRANE PROTEIN / PROTON TRANSPORT / ion transport / proton pump / P-type ATPase / active transport | ||||||
機能・相同性 | ![]() P-type H+-exporting transporter / proton export across plasma membrane / P-type proton-exporting transporter activity / proton transmembrane transport / regulation of intracellular pH / membrane => GO:0016020 / ATP hydrolysis activity / ATP binding / metal ion binding / plasma membrane 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子線結晶学 / クライオ電子顕微鏡法 / 解像度: 8 Å | ||||||
![]() | Kuhlbrandt, W. | ||||||
![]() | ![]() タイトル: Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase. 著者: Werner Kühlbrandt / Johan Zeelen / Jens Dietrich / ![]() 要旨: Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic ...Proton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by approximately 70 degrees to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation. #1: ![]() タイトル: Three-dimensional map of the plasma membrane H+-ATPase in the open conformation 著者: AUER, M. / SCARBOROUGH, G.A. / KUHLBRANDT, W. | ||||||
履歴 |
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Remark 295 | NON-CRYSTALLOGRAPHIC SYMMETRY THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW DESCRIBE ... NON-CRYSTALLOGRAPHIC SYMMETRY THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH ATOMS ARE NOT FOUND IN THE ENTRY. APPLIED TO TRANSFORMED TO TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD SSS M 1 A 1 .. 920 B 1 .. 920 ? WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS | ||||||
Remark 300 | BIOMOLECULE: 1 THIS ENTRY CONTAINS A PORTION OF THE BIOLOGICALLY SIGNIFICANT MULTIMER. SEE REMARK ...BIOMOLECULE: 1 THIS ENTRY CONTAINS A PORTION OF THE BIOLOGICALLY SIGNIFICANT MULTIMER. SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S) ASSEMBLY COMPONENTS COM_ID: 1 NAME:PLASMA MEMBRANE PROTON ATPASE HEXAMERIC ASSEMBLY |
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構造の表示
ムービー |
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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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PDBx/mmCIF形式 | ![]() | 317.1 KB | 表示 | ![]() |
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PDB形式 | ![]() | 249.7 KB | 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
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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非結晶学的対称性 (NCS) | NCS oper: (Code: given / Matrix: (0.5, 0.866), |
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要素
#1: タンパク質 | 分子量: 99984.359 Da / 分子数: 2 / 由来タイプ: 天然 詳細: isolated from plasma membrane of cultured Neurospora cells 由来: (天然) ![]() |
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-実験情報
-実験
実験 | 手法: 電子線結晶学 |
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EM実験 | 試料の集合状態: 2D ARRAY / 3次元再構成法: 電子線結晶学 |
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試料調製
構成要素 |
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緩衝液 | 名称: 100 mM ammonium sulphate, Tris-HCl, 30% glycerol, 10.5% PEG 4000 pH: 6.8 詳細: 100 mM ammonium sulphate, Tris-HCl, 30% glycerol, 10.5% PEG 4000 | |||||||||||||||
試料 | 濃度: 1 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | |||||||||||||||
試料支持 | 詳細: hydrophobic carbon support film on 400 mesh gold-plated Cu EM grid | |||||||||||||||
急速凍結 | 詳細: 2D crystals were vitrified by immersion in liquid nitrogen | |||||||||||||||
結晶化 | *PLUS 手法: other / 詳細: MRC ELECTRON CRYSTALLOGRAPHY |
-データ収集
顕微鏡 | モデル: JEOL 3000SFF 詳細: Images were also recorded on JEOL 2000 EX and Philips CM200 FEG electron microscopes at 80 K at a dose of 1000 e/nm**2 |
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電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 50000 X / 倍率(補正後): 50000 X / 最大 デフォーカス(公称値): 1200 nm / 最小 デフォーカス(公称値): 600 nm / Cs: 1.6 mm |
試料ホルダ | 温度: 4 K / 傾斜角・最大: 60 ° / 傾斜角・最小: 0 ° |
撮影 | 電子線照射量: 25 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM |
画像スキャン | デジタル画像の数: 60 |
放射 | 散乱光タイプ: electron |
放射波長 | 相対比: 1 |
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解析
EMソフトウェア | 名称: MRC / カテゴリ: 3次元再構成 | ||||||||||||
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CTF補正 | 詳細: crystallographic | ||||||||||||
3次元再構成 | 解像度: 8 Å / ピクセルサイズ(公称値): 1.4 Å / ピクセルサイズ(実測値): 1.4 Å / 倍率補正: electron diffraction of standard specimen / 対称性のタイプ: 2D CRYSTAL | ||||||||||||
原子モデル構築 | プロトコル: OTHER / 空間: REAL / Target criteria: best visual fit using the program o / 詳細: METHOD--manual REFINEMENT PROTOCOL--manual fit | ||||||||||||
原子モデル構築 | 詳細: this entry | ||||||||||||
精密化 | 最高解像度: 8 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 8 Å
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