+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-26612 | ||||||||||||||||||
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タイトル | Complex of UBE2O with NAP1L1 and ubiquitylated uL2 | ||||||||||||||||||
マップデータ | Sharpened map | ||||||||||||||||||
試料 |
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キーワード | Ubiquitylation (ユビキチン) / CYTOSOLIC PROTEIN (細胞質基質) | ||||||||||||||||||
機能・相同性 | 機能・相同性情報 histone chaperone activity / (E3-independent) E2 ubiquitin-conjugating enzyme / positive regulation of neural precursor cell proliferation / positive regulation of BMP signaling pathway / retrograde transport, endosome to Golgi / positive regulation of neurogenesis / ヒドロキシル化 / protein monoubiquitination / ubiquitin conjugating enzyme activity / Peptide chain elongation ...histone chaperone activity / (E3-independent) E2 ubiquitin-conjugating enzyme / positive regulation of neural precursor cell proliferation / positive regulation of BMP signaling pathway / retrograde transport, endosome to Golgi / positive regulation of neurogenesis / ヒドロキシル化 / protein monoubiquitination / ubiquitin conjugating enzyme activity / Peptide chain elongation / protein K63-linked ubiquitination / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / グリコーゲン合成 / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Constitutive Signaling by NOTCH1 HD Domain Mutants / Endosomal Sorting Complex Required For Transport (ESCRT) / NOTCH2 Activation and Transmission of Signal to the Nucleus / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / Downregulation of ERBB4 signaling / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Pexophagy / InlA-mediated entry of Listeria monocytogenes into host cells / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / NF-kB is activated and signals survival / Regulation of PTEN localization / Regulation of BACH1 activity / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLK / MAP3K8 (TPL2)-dependent MAPK1/3 activation / cytosolic ribosome / TICAM1, RIP1-mediated IKK complex recruitment / Gap-filling DNA repair synthesis and ligation in GG-NER / Downregulation of TGF-beta receptor signaling / Translesion synthesis by POLI / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Regulation of NF-kappa B signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / NOTCH3 Activation and Transmission of Signal to the Nucleus / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Negative regulators of DDX58/IFIH1 signaling / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A 類似検索 - 分子機能 | ||||||||||||||||||
生物種 | 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: 3.5 Å | ||||||||||||||||||
データ登録者 | Yip MCJ / Sedor SF / Shao S | ||||||||||||||||||
資金援助 | 米国, 5件
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引用 | ジャーナル: Nat Struct Mol Biol / 年: 2022 タイトル: Mechanism of client selection by the protein quality-control factor UBE2O. 著者: Matthew C J Yip / Samantha F Sedor / Sichen Shao / 要旨: The E2/E3 enzyme UBE2O ubiquitylates diverse clients to mediate important processes, including targeting unassembled 'orphan' proteins for quality control and clearing ribosomes during erythropoiesis. ...The E2/E3 enzyme UBE2O ubiquitylates diverse clients to mediate important processes, including targeting unassembled 'orphan' proteins for quality control and clearing ribosomes during erythropoiesis. How quality-control factors, such as UBE2O, select clients on the basis of heterogeneous features is largely unknown. Here, we show that UBE2O client selection is regulated by ubiquitin binding and a cofactor, NAP1L1. Attaching a single ubiquitin onto a client enhances UBE2O binding and multi-mono-ubiquitylation. UBE2O also repurposes the histone chaperone NAP1L1 as an adapter to recruit a subset of clients. Cryo-EM structures of human UBE2O in complex with NAP1L1 reveal a malleable client recruitment interface that is autoinhibited by the intrinsically reactive UBC domain. Adding a ubiquitylated client identifies a distinct ubiquitin-binding SH3-like domain required for client selection. Our findings reveal how multivalency and a feed-forward mechanism drive the selection of protein quality-control clients. | ||||||||||||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_26612.map.gz | 119.7 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-26612-v30.xml emd-26612.xml | 21.1 KB 21.1 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_26612_fsc.xml | 11.3 KB | 表示 | FSCデータファイル |
画像 | emd_26612.png | 98 KB | ||
Filedesc metadata | emd-26612.cif.gz | 6.7 KB | ||
その他 | emd_26612_additional_1.map.gz emd_26612_additional_2.map.gz emd_26612_half_map_1.map.gz emd_26612_half_map_2.map.gz | 112.5 MB 71.9 MB 118 MB 118 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-26612 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26612 | 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_26612.map.gz / 形式: CCP4 / 大きさ: 149.9 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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注釈 | Sharpened map | ||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.825 Å | ||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-追加マップ: deepEMhancer sharpened map
ファイル | emd_26612_additional_1.map | ||||||||||||
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注釈 | deepEMhancer sharpened map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-追加マップ: Unsharpened map
ファイル | emd_26612_additional_2.map | ||||||||||||
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注釈 | Unsharpened map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map 2
ファイル | emd_26612_half_map_1.map | ||||||||||||
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注釈 | Half map 2 | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map 1
ファイル | emd_26612_half_map_2.map | ||||||||||||
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注釈 | Half map 1 | ||||||||||||
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 : Complex of UBE2O with NAP1L1 and ubiquitylated uL2
全体 | 名称: Complex of UBE2O with NAP1L1 and ubiquitylated uL2 |
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要素 |
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-超分子 #1: Complex of UBE2O with NAP1L1 and ubiquitylated uL2
超分子 | 名称: Complex of UBE2O with NAP1L1 and ubiquitylated uL2 / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #2 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-...
分子 | 名称: Ubiquitin,60S ribosomal protein L8,(E3-independent) E2 ubiquitin-conjugating enzyme fusion タイプ: protein_or_peptide / ID: 1 / コピー数: 2 / 光学異性体: LEVO / EC番号: (E3-independent) E2 ubiquitin-conjugating enzyme |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 190.728406 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: MASWSHPQFE KGAWSHPQFE KGSWSHPQFE KGPAGSENLY FQGSGIRMQI FVKTLTGKTI TLEVEPSDTI ENVKAKIQDK EGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGVGSMGRV IRGQRKGAGS VFRAHVKHRK GAARLRAVDF A ERHGYIKG ...文字列: MASWSHPQFE KGAWSHPQFE KGSWSHPQFE KGPAGSENLY FQGSGIRMQI FVKTLTGKTI TLEVEPSDTI ENVKAKIQDK EGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGVGSMGRV IRGQRKGAGS VFRAHVKHRK GAARLRAVDF A ERHGYIKG IVKDIIHDPG RGAPLAKVVF RDPYRFKKRT ELFIAAEGIH TGQFVYCGKK AQLNVGNVLP VGTMPEGTIV CC LEEKPGD RGKLARASGN YATVISHNPE TKKTRVKLPS GSKKVISSAN RAVVGVVAGG GRIDKPILKA GRAYHKYKAK RNC WPRVRG VAMNPVEHPF GGGNHQHIGK PSTIRRDAPA GRKVGLIAAR RTGRLRGTKT VQEKENGGSG LEVLFQGPGG SGGG SGLEV LFQGPGGSGY PYDVPDYAGY PYDVPDYAGS YPYDVPDYAG SAIRDRTMAD PAAPTPAAPA PAQAPAPAPE AVPAP AAAP VPAPAPASDS ASGPSSDSGP EAGSQRLLFS HDLVSGRYRG SVHFGLVRLI HGEDSDSEGE EEGRGSSGCS EAGGAG HEE GRASPLRRGY VRVQWYPEGV KQHVKETKLK LEDRSVVPRD VVRHMRSTDS QCGTVIDVNI DCAVKLIGTN CIIYPVN SK DLQHIWPFMY GDYIAYDCWL GKVYDLKNQI ILKLSNGARC SMNTEDGAKL YDVCPHVSDS GLFFDDSYGF YPGQVLIG P AKIFSSVQWL SGVKPVLSTK SKFRVVVEEV QVVELKVTWI TKSFCPGGTD SVSPPPSVIT QENLGRVKRL GCFDHAQRQ LGERCLYVFP AKVEPAKIAW ECPEKNCAQG EGSMAKKVKR LLKKQVVRIM SCSPDTQCSR DHSMEDPDKK GESKTKSEAE SASPEETPD GSASPVEMQD EGAEEPHEAG EQLPPFLLKE GRDDRLHSAE QDADDEAADD TDDTSSVTSS ASSTTSSQSG S GTSRKKSI PLSIKNLKRK HKRKKNKITR DFKPGDRVAV EVVTTMTSAD VMWQDGSVEC NIRSNDLFPV HHLDNNEFCP GD FVVDKRV QSCPDPAVYG VVQSGDHIGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT EDG APHKED EPSVGQVARV DVSSKVEVVW ADNSKTIILP QHLYNIESEI EESDYDSVEG STSGASSDEW EDDSDSWETD NGLV EDEHP KIEEPPIPPL EQPVAPEDKG VVISEEAATA AVQGAVAMAA PMAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMT VEQL LTGSPTSPTV EPEKPTREKK FLDDIKKLQE NLKKTLDNVA IVEEEKMEAV PDVERKEDKP EGQSPVKAEW PSETPV LCQ QCGGKPGVTF TSAKGEVFSV LEFAPSNHSF KKIEFQPPEA KKFFSTVRKE MALLATSLPE GIMVKTFEDR MDLFSAL IK GPTRTPYEDG LYLFDIQLPN IYPAVPPHFC YLSQCSGRLN PNLYDNGKVK VSLLGTWIGK GTERWTSKSS LLQVLISI Q GLILVNEPYY NEAGFDSDRG LQEGYENSRC YNEMALIRVV QSMTQLVRRP PEVFEQEIRQ HFSTGGWRLV NRIESWLET HALLEKAQAL PNGVPKASSS PEPPAVAELS DSGQQEPEDG GPAPGEASQG SDSEGGAQGL ASASRDHTDQ TSETAPDASV PPSVKPKKR RKSYRSFLPE KSGYPDIGFP LFPLSKGFIK SIRGVLTQFR AALLEAGMPE CTEDK UniProtKB: Ubiquitin-ribosomal protein eL40 fusion protein, Large ribosomal subunit protein uL2, (E3-independent) E2 ubiquitin-conjugating enzyme |
-分子 #2: Nucleosome assembly protein 1-like 1
分子 | 名称: Nucleosome assembly protein 1-like 1 / タイプ: protein_or_peptide / ID: 2 / コピー数: 2 / 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: 48.363898 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: MDYKDHDGDY KDHDIDYKDD DDKAGSADID NKEQSELDQD LDDVEEVEEE ETGEETKLKA RQLTVQMMQN PQILAALQER LDGLVETPT GYIESLPRVV KRRVNALKNL QVKCAQIEAK FYEEVHDLER KYAVLYQPLF DKRFEIINAI YEPTEEECEW K PDEEDEIS ...文字列: MDYKDHDGDY KDHDIDYKDD DDKAGSADID NKEQSELDQD LDDVEEVEEE ETGEETKLKA RQLTVQMMQN PQILAALQER LDGLVETPT GYIESLPRVV KRRVNALKNL QVKCAQIEAK FYEEVHDLER KYAVLYQPLF DKRFEIINAI YEPTEEECEW K PDEEDEIS EELKEKAKIE DEKKDEEKED PKGIPEFWLT VFKNVDLLSD MVQEHDEPIL KHLKDIKVKF SDAGQPMSFV LE FHFEPNE YFTNEVLTKT YRMRSEPDDS DPFSFDGPEI MGCTGCQIDW KKGKNVTLKT IKKKQKHKGR GTVRTVTKTV SND SFFNFF APPEVPESGD LDDDAEAILA ADFEIGHFLR ERIIPRSVLY FTGEAIEDDD DDYDEEGEEA DEEGEEEGDE ENDP DYDPK KDQNPAECKQ Q UniProtKB: Nucleosome assembly protein 1-like 1 |
-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
濃度 | 1 mg/mL |
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緩衝液 | pH: 7.5 |
凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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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: FLOOD BEAM / 撮影モード: BRIGHT FIELDBright-field microscopy / 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): 1.4000000000000001 µm |
撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 59.6 e/Å2 |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |