+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-13159 | |||||||||
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タイトル | Structure of the V. vulnificus ExoY-G-actin-profilin complex | |||||||||
マップデータ | Main map, was used to build VvExoY and Actin | |||||||||
試料 |
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機能・相同性 | 機能・相同性情報 calcium- and calmodulin-responsive adenylate cyclase activity / synapse maturation / modification of postsynaptic actin cytoskeleton / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / negative regulation of actin filament bundle assembly / adenyl-nucleotide exchange factor activity / regulation of transepithelial transport / morphogenesis of a polarized epithelium / : ...calcium- and calmodulin-responsive adenylate cyclase activity / synapse maturation / modification of postsynaptic actin cytoskeleton / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / negative regulation of actin filament bundle assembly / adenyl-nucleotide exchange factor activity / regulation of transepithelial transport / morphogenesis of a polarized epithelium / : / bBAF complex / postsynaptic actin cytoskeleton organization / npBAF complex / protein localization to adherens junction / nBAF complex / postsynaptic actin cytoskeleton / brahma complex / Tat protein binding / negative regulation of actin filament polymerization / positive regulation of actin filament bundle assembly / structural constituent of postsynaptic actin cytoskeleton / GBAF complex / regulation of G0 to G1 transition / Signaling by ROBO receptors / regulation of actin filament polymerization / Formation of annular gap junctions / dense body / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / regulation of double-strand break repair / regulation of nucleotide-excision repair / adherens junction assembly / RSC-type complex / Prefoldin mediated transfer of substrate to CCT/TriC / positive regulation of ATP-dependent activity / RHOF GTPase cycle / Adherens junctions interactions / proline-rich region binding / tight junction / PCP/CE pathway / positive regulation of ruffle assembly / regulation of mitotic metaphase/anaphase transition / Interaction between L1 and Ankyrins / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / SWI/SNF complex / regulation of norepinephrine uptake / positive regulation of double-strand break repair / positive regulation of T cell differentiation / regulation of synaptic vesicle endocytosis / negative regulation of stress fiber assembly / apical junction complex / host cell cytosol / positive regulation of actin filament polymerization / establishment or maintenance of cell polarity / regulation of cyclin-dependent protein serine/threonine kinase activity / cortical cytoskeleton / maintenance of blood-brain barrier / NuA4 histone acetyltransferase complex / positive regulation of epithelial cell migration / positive regulation of stem cell population maintenance / detection of maltose stimulus / nitric-oxide synthase binding / maltose transport complex / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of G1/S transition of mitotic cell cycle / Recycling pathway of L1 / brush border / carbohydrate transport / kinesin binding / negative regulation of cell differentiation / maltose binding / calyx of Held / maltose transport / maltodextrin transmembrane transport / actin monomer binding / positive regulation of double-strand break repair via homologous recombination / carbohydrate transmembrane transporter activity / EPH-ephrin mediated repulsion of cells / positive regulation of myoblast differentiation / regulation of protein localization to plasma membrane / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / phosphatidylinositol-4,5-bisphosphate binding / substantia nigra development / EPHB-mediated forward signaling / phosphotyrosine residue binding / axonogenesis / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / platelet aggregation / negative regulation of protein binding / neural tube closure / cell motility / Translocation of SLC2A4 (GLUT4) to the plasma membrane / actin filament 類似検索 - 分子機能 | |||||||||
生物種 | Vibrio vulnificus (バクテリア) / Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.9 Å | |||||||||
データ登録者 | Belyy A / Merino F / Raunser S | |||||||||
資金援助 | ドイツ, 1件
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引用 | ジャーナル: Nat Commun / 年: 2021 タイトル: Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens. 著者: Alexander Belyy / Felipe Merino / Undine Mechold / Stefan Raunser / 要旨: Bacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this ...Bacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this activation is, however, unclear. Here, we report structures of ExoY from Pseudomonas aeruginosa and Vibrio vulnificus bound to their corresponding activators F-actin and profilin-G-actin. The structures reveal that in contrast to the apo-state, two flexible regions become ordered and interact strongly with actin. The specific stabilization of these regions results in an allosteric stabilization of the nucleotide binding pocket and thereby to an activation of the enzyme. Differences in the sequence and conformation of the actin-binding regions are responsible for the selective binding to either F- or G-actin. Other nucleotidyl cyclase toxins that bind to calmodulin rather than actin undergo a similar disordered-to-ordered transition during activation, suggesting that the allosteric activation-by-stabilization mechanism of ExoY is conserved in these enzymes, albeit the different activator. | |||||||||
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 | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_13159.map.gz | 7.5 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-13159-v30.xml emd-13159.xml | 17.1 KB 17.1 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_13159_fsc.xml | 12.4 KB | 表示 | FSCデータファイル |
画像 | emd_13159.png | 117.9 KB | ||
その他 | emd_13159_additional_1.map.gz | 7.3 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-13159 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13159 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_13159_validation.pdf.gz | 323.7 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_13159_full_validation.pdf.gz | 323.2 KB | 表示 | |
XML形式データ | emd_13159_validation.xml.gz | 11.9 KB | 表示 | |
CIF形式データ | emd_13159_validation.cif.gz | 16 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13159 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13159 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_13159.map.gz / 形式: CCP4 / 大きさ: 125 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Main map, was used to build VvExoY and Actin | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.68 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-追加マップ: Secondary map, was used to build actin-profilin interface
ファイル | emd_13159_additional_1.map | ||||||||||||
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注釈 | Secondary map, was used to build actin-profilin interface | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
-全体 : Structure of the V. vulnificus ExoY-G-actin-profilin complex
全体 | 名称: Structure of the V. vulnificus ExoY-G-actin-profilin complex |
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要素 |
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-超分子 #1: Structure of the V. vulnificus ExoY-G-actin-profilin complex
超分子 | 名称: Structure of the V. vulnificus ExoY-G-actin-profilin complex タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#3 |
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-分子 #1: Maltose/maltodextrin-binding periplasmic protein,RTX-toxin
分子 | 名称: Maltose/maltodextrin-binding periplasmic protein,RTX-toxin タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Vibrio vulnificus (バクテリア) |
分子量 | 理論値: 91.467539 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: MGSSHHHHHH SSGLVPRGSH MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFG GYAQSGLLAE ITPDKAFQDK LYPFTWDAVR YNGKLIAYPI AVEALSLIYN KDLLPNPPKT WEEIPALDKE L KAKGKSAL ...文字列: MGSSHHHHHH SSGLVPRGSH MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFG GYAQSGLLAE ITPDKAFQDK LYPFTWDAVR YNGKLIAYPI AVEALSLIYN KDLLPNPPKT WEEIPALDKE L KAKGKSAL MFNLQEPYFT WPLIAADGGY AFKYENGKYD IKDVGVDNAG AKAGLTFLVD LIKNKHMNAD TDYSIAEAAF NK GETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPL GAVALK SYEEELVKDP RIAATMENAQ KGEIMPNIPQ MSAFWYAVRT AVINAASGRQ TVDEALKDAQ TNSGSSGSSV EASD TELGT NTDAPHKNYQ SRDLVLEPIV QPETIELGMP DSDQKILAEV AERENVIIGV RPVDEKSKSL IDSKLYSSKG LFVKA KSSD WGPMSGFIPV DQAFAKASAR RDLDKFNGYA EQSIESGNAV SADLYLNQVR IDELVSKYQS LTALEFDAES GMYKTT ATN GDQTVTFFLN KVTVDSKDLW QVHYIKDGKL APFKVIGDPV SKQPMTADYD LLTVMYSYSD LGPQDKLKQP LTWEQWK ES VTYEELTPKY KELYNSEVLY NKKDGASLGV VSDRLKALKD VINTSLGRTD GLEMVHHGAD DANPYAVMAD NFPATFFV P KSFFMEDGLG EGKGSIQTYF NVNEQGAVVI RDPQEFSNFQ QVAINVSYRA SLNDKWNVGL DDPLFTPKSK LSHDFLNAK EEVIKKLSGE VETNVRTTQL LTDNEGL |
-分子 #2: Actin, cytoplasmic 1
分子 | 名称: Actin, cytoplasmic 1 / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 41.402242 KDa |
組換発現 | 生物種: Trichoplusia ni (イラクサキンウワバ) |
配列 | 文字列: DIAALVVDNG SGMCKAGFAG DDAPRAVFPS IVGRPRHQGV MVGMGQKDSY VGDEAQSKRG ILTLKYPIE(HIC) GIVTNW DDM EKIWHHTFYN ELRVAPEEHP VLLTEAPLNP KANREKMTQI MFETFNTPAM YVAIQAVLSL YASGRTTGIV MDSGDGV TH ...文字列: DIAALVVDNG SGMCKAGFAG DDAPRAVFPS IVGRPRHQGV MVGMGQKDSY VGDEAQSKRG ILTLKYPIE(HIC) GIVTNW DDM EKIWHHTFYN ELRVAPEEHP VLLTEAPLNP KANREKMTQI MFETFNTPAM YVAIQAVLSL YASGRTTGIV MDSGDGV TH TVPIYEGYAL PHAILRLDLA GRDLTDYLMK ILTERGYSFT TTAEREIVRD IKEKLCYVAL DFEQEMATAA SSSSLEKS Y ELPDGQVITI GNERFRCPEA LFQPSFLGME SAGIHETTFN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPSI VHRKCF |
-分子 #3: Profilin-1
分子 | 名称: Profilin-1 / タイプ: protein_or_peptide / ID: 3 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 15.071222 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLR TKSTGGAPTF NVTVTKTDKT LVLLMGKEGV HGGLINKKCY EMASHLRRSQ Y |
-分子 #4: CALCIUM ION
分子 | 名称: CALCIUM ION / タイプ: ligand / ID: 4 / コピー数: 1 / 式: CA |
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分子量 | 理論値: 40.078 Da |
-分子 #5: ADENOSINE-5'-TRIPHOSPHATE
分子 | 名称: ADENOSINE-5'-TRIPHOSPHATE / タイプ: ligand / ID: 5 / コピー数: 1 / 式: ATP |
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分子量 | 理論値: 507.181 Da |
Chemical component information | ChemComp-ATP: |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 8 |
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グリッド | モデル: Quantifoil R2/1 / 材質: COPPER / メッシュ: 300 |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / 装置: FEI VITROBOT MARK III |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 検出モード: SUPER-RESOLUTION / 撮影したグリッド数: 1 / 実像数: 6879 / 平均露光時間: 2.0 sec. / 平均電子線量: 60.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: SPOT SCAN / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 1.2 µm |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |