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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: 9c62 | ||||||||||||||||||
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タイトル | P400 subcomplex of the native human TIP60 complex | ||||||||||||||||||
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![]() | GENE REGULATION / complex / chromatin regulator | ||||||||||||||||||
機能・相同性 | ![]() ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / regulation of transepithelial transport / histone chaperone activity / sperm DNA condensation ...ATP-dependent H2AZ histone chaperone activity / piccolo histone acetyltransferase complex / promoter-enhancer loop anchoring activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / regulation of transepithelial transport / histone chaperone activity / sperm DNA condensation / establishment of protein localization to chromatin / morphogenesis of a polarized epithelium / bBAF complex / postsynaptic actin cytoskeleton organization / npBAF complex / nBAF complex / protein localization to adherens junction / R2TP complex / brahma complex / postsynaptic actin cytoskeleton / dynein axonemal particle / Tat protein binding / structural constituent of postsynaptic actin cytoskeleton / chromatin-protein adaptor activity / RPAP3/R2TP/prefoldin-like complex / GBAF complex / protein antigen binding / dense body / Formation of annular gap junctions / Swr1 complex / regulation of G0 to G1 transition / neural retina development / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / apical protein localization / regulation of double-strand break repair / adherens junction assembly / regulation of nucleotide-excision repair / Ino80 complex / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / blastocyst formation / RHOF GTPase cycle / Regulation of MITF-M-dependent genes involved in pigmentation / Adherens junctions interactions / tight junction / enzyme-substrate adaptor activity / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / Interaction between L1 and Ankyrins / protein folding chaperone complex / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / SWI/SNF complex / box C/D snoRNP assembly / ATP-dependent chromatin remodeler activity / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / apical junction complex / positive regulation of T cell differentiation / establishment or maintenance of cell polarity / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / regulation of cyclin-dependent protein serine/threonine kinase activity / negative regulation of gene expression, epigenetic / spinal cord development / cortical cytoskeleton / maintenance of blood-brain barrier / regulation of chromosome organization / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Transcriptional Regulation by E2F6 / regulation of DNA replication / regulation of G1/S transition of mitotic cell cycle / Recycling pathway of L1 / kinesin binding / brush border / somatic stem cell population maintenance / calyx of Held / TFIID-class transcription factor complex binding / negative regulation of cell differentiation / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / spermatid development / positive regulation of double-strand break repair via homologous recombination / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RNA polymerase II core promoter sequence-specific DNA binding / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of myoblast differentiation / heterochromatin / Replacement of protamines by nucleosomes in the male pronucleus / regulation of DNA repair / Packaging Of Telomere Ends / histone acetyltransferase activity 類似検索 - 分子機能 | ||||||||||||||||||
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: 5.28 Å | ||||||||||||||||||
![]() | Yang, Z. / Mameri, A. / Florez Ariza, A.J. / Cote, J. / Nogales, E. | ||||||||||||||||||
資金援助 | ![]() ![]()
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![]() | ![]() タイトル: Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. 著者: Zhenlin Yang / Amel Mameri / Claudia Cattoglio / Catherine Lachance / Alfredo Jose Florez Ariza / Jie Luo / Jonathan Humbert / Deepthi Sudarshan / Arul Banerjea / Maxime Galloy / Amélie ...著者: Zhenlin Yang / Amel Mameri / Claudia Cattoglio / Catherine Lachance / Alfredo Jose Florez Ariza / Jie Luo / Jonathan Humbert / Deepthi Sudarshan / Arul Banerjea / Maxime Galloy / Amélie Fradet-Turcotte / Jean-Philippe Lambert / Jeff A Ranish / Jacques Côté / Eva Nogales / ![]() ![]() 要旨: The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to regulate ...The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the EP400 subunit serves as a scaffold holding the different functional modules in specific positions, creating a unique arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly. | ||||||||||||||||||
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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 | ![]() | 1.7 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 | ![]() 45240MC ![]() 9c47C ![]() 9c4bC ![]() 9c57C ![]() 9c6nC 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 , 10種, 15分子 BDFCEAGHIJKLMNO
#1: タンパク質 | 分子量: 51222.465 Da / 分子数: 3 / 由来タイプ: 天然 / 由来: (天然) ![]() #2: タンパク質 | 分子量: 50296.914 Da / 分子数: 3 / 由来タイプ: 天然 / 由来: (天然) ![]() #3: タンパク質 | | 分子量: 343867.312 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() 参照: UniProt: Q96L91, 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 #4: タンパク質 | | 分子量: 93589.172 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #5: タンパク質 | | 分子量: 53090.699 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #6: タンパク質 | | 分子量: 41782.660 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #7: タンパク質 | | 分子量: 40658.363 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #8: タンパク質 | 分子量: 47509.812 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #9: タンパク質 | | 分子量: 13581.796 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() #10: タンパク質 | | 分子量: 13981.267 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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-非ポリマー , 1種, 6分子 ![](data/chem/img/ADP.gif)
#11: 化合物 | ChemComp-ADP / |
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-詳細
研究の焦点であるリガンドがあるか | 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: Reconstituted P400 Subcomplex of the human TIP60 complex タイプ: COMPLEX / Entity ID: #8, #1-#7, #9-#10 / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 7.5 |
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: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: 4D-STEM / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 1000 nm |
撮影 | 電子線照射量: 50 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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解析
EMソフトウェア | 名称: PHENIX / バージョン: 1.20.1_4487: / カテゴリ: モデル精密化 |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3次元再構成 | 解像度: 5.28 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 22686 / 対称性のタイプ: POINT |
精密化 | 交差検証法: NONE |