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基本情報
登録情報 | データベース: EMDB / ID: EMD-10960 | |||||||||
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タイトル | Cryo-EM structure of the ARP2/3 1A5C isoform complex. | |||||||||
![]() | Cryo-EM structure of the human Arp2/3 1A5C isoform complex. | |||||||||
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![]() | Cytoskeleton / STRUCTURAL PROTEIN | |||||||||
機能・相同性 | ![]() meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / spindle localization / actin polymerization-dependent cell motility / Arp2/3 protein complex / asymmetric cell division / Arp2/3 complex-mediated actin nucleation ...meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / muscle cell projection membrane / meiotic cytokinesis / spindle localization / actin polymerization-dependent cell motility / Arp2/3 protein complex / asymmetric cell division / Arp2/3 complex-mediated actin nucleation / actin nucleation / actin cap / regulation of actin filament polymerization / membrane organization / establishment or maintenance of cell polarity / positive regulation of actin filament polymerization / Fc-gamma receptor signaling pathway involved in phagocytosis / filamentous actin / brush border / positive regulation of double-strand break repair via homologous recombination / cilium assembly / ephrin receptor signaling pathway / RHO GTPases Activate WASPs and WAVEs / positive regulation of lamellipodium assembly / positive regulation of substrate adhesion-dependent cell spreading / EPHB-mediated forward signaling / actin filament polymerization / cellular response to nerve growth factor stimulus / cell projection / FCGR3A-mediated phagocytosis / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / cellular response to type II interferon / actin filament binding / azurophil granule lumen / cell-cell junction / Clathrin-mediated endocytosis / actin cytoskeleton / cell migration / lamellipodium / site of double-strand break / actin binding / cell cortex / actin cytoskeleton organization / secretory granule lumen / ficolin-1-rich granule lumen / endosome / neuron projection / focal adhesion / glutamatergic synapse / Neutrophil degranulation / enzyme binding / positive regulation of transcription by RNA polymerase II / extracellular exosome / extracellular region / nucleoplasm / ATP binding / membrane / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 | |||||||||
生物種 | ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.5 Å | |||||||||
![]() | von Loeffelholz O / Moores C | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms. 著者: Ottilie von Loeffelholz / Andrew Purkiss / Luyan Cao / Svend Kjaer / Naoko Kogata / Guillaume Romet-Lemonne / Michael Way / Carolyn A Moores / ![]() ![]() 要旨: The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce ...The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 Å resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes. | |||||||||
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「今月の分子」の関連する項目 |
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注釈 | Cryo-EM structure of the human Arp2/3 1A5C isoform complex. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.09 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
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試料の構成要素
-全体 : human ARP2/3 1A5C isoform complex
全体 | 名称: human ARP2/3 1A5C isoform complex |
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要素 |
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-超分子 #1: human ARP2/3 1A5C isoform complex
超分子 | 名称: human ARP2/3 1A5C isoform complex / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#7 |
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由来(天然) | 生物種: ![]() |
-分子 #1: Actin-related protein 3
分子 | 名称: Actin-related protein 3 / 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: ![]() |
分子量 | 理論値: 47.428031 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLM ERFMEQVIFK YLRAEPEDHY FLLTEPPLNT PENREYTAEI MFESFNVPGL YIAVQAVLAL AASWTSRQVG E RTLTGTVI ...文字列: MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLM ERFMEQVIFK YLRAEPEDHY FLLTEPPLNT PENREYTAEI MFESFNVPGL YIAVQAVLAL AASWTSRQVG E RTLTGTVI DSGDGVTHVI PVAEGYVIGS CIKHIPIAGR DITYFIQQLL RDREVGIPPE QSLETAKAVK ERYSYVCPDL VK EFNKYDT DGSKWIKQYT GINAISKKEF SIDVGYERFL GPEIFFHPEF ANPDFTQPIS EVVDEVIQNC PIDVRRPLYK NIV LSGGST MFRDFGRRLQ RDLKRTVDAR LKLSEELSGG RLKPKPIDVQ VITHHMQRYA VWFGGSMLAS TPEFYQVCHT KKDY EEIGP SICRHNPVFG VMS UniProtKB: Actin-related protein 3 |
-分子 #2: Actin-related protein 2/3 complex subunit 2
分子 | 名称: Actin-related protein 2/3 complex subunit 2 / 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: ![]() |
分子量 | 理論値: 34.386043 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS LKFYKELQAH GADELLKRVY GSFLVNPES GYNVSLLYDL ENLPASKDSI VHQAGMLKRN CFASVFEKYF QFQEEGKEGE NRAVIHYRDD ETMYVESKKD R VTVVFSTV ...文字列: MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS LKFYKELQAH GADELLKRVY GSFLVNPES GYNVSLLYDL ENLPASKDSI VHQAGMLKRN CFASVFEKYF QFQEEGKEGE NRAVIHYRDD ETMYVESKKD R VTVVFSTV FKDDDDVVIG KVFMQEFKEG RRASHTAPQV LFSHREPPLE LKDTDAAVGD NIGYITFVLF PRHTNASARD NT INLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR UniProtKB: Actin-related protein 2/3 complex subunit 2 |
-分子 #3: Actin-related protein 2/3 complex subunit 3
分子 | 名称: Actin-related protein 2/3 complex subunit 3 / 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: ![]() |
分子量 | 理論値: 20.572666 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKS QGEKEMYTLG ITNFPIPGEP GFPLNAIYAK PANKQEDEVM RAYLQQLRQE TGLRLCEKVF DPQNDKPSKW W TCFVKRQF MNKSLSGPGQ UniProtKB: Actin-related protein 2/3 complex subunit 3 |
-分子 #4: Actin-related protein 2
分子 | 名称: Actin-related protein 2 / タイプ: protein_or_peptide / ID: 4 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
分子量 | 理論値: 44.818711 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPAIVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLW DYTFGPEKLN IDTRNCKILL TEPPMNPTKN REKIVEVMFE TYQFSGVYVA IQAVLTLYAQ GLLTGVVVDS G DGVTHICP ...文字列: MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPAIVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLW DYTFGPEKLN IDTRNCKILL TEPPMNPTKN REKIVEVMFE TYQFSGVYVA IQAVLTLYAQ GLLTGVVVDS G DGVTHICP VYEGFSLPHL TRRLDIAGRD ITRYLIKLLL LRGYAFNHSA DFETVRMIKE KLCYVGYNIE QEQKLALETT VL VESYTLP DGRIIKVGGE RFEAPEALFQ PHLINVEGVG VAELLFNTIQ AADIDTRSEF YKHIVLSGGS TMYPGLPSRL ERE LKQLYL ERVLKGDVEK LSKFKIRIED PPRRKHMVFL GGAVLADIMK DKDNFWMTRQ EYQEKGVRVL EKLGVTVR UniProtKB: Actin-related protein 2 |
-分子 #5: Actin-related protein 2/3 complex subunit 4
分子 | 名称: Actin-related protein 2/3 complex subunit 4 / タイプ: protein_or_peptide / ID: 5 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
分子量 | 理論値: 19.697047 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHK FMRFMMMRAE NFFILRRKPV EGYDISFLIT NFHTEQMYKH KLVDFVIHFM EEIDKEISEM KLSVNARARI V AEEFLKNF UniProtKB: Actin-related protein 2/3 complex subunit 4 |
-分子 #6: Actin-related protein 2/3 complex subunit 5
分子 | 名称: Actin-related protein 2/3 complex subunit 5 / タイプ: protein_or_peptide / ID: 6 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
分子量 | 理論値: 16.341407 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAN DIEKAVQSLD KNGVDLLMKY IYKGFESPSD NSSAMLLQWH EKALAAGGVG SIVRVLTARK TV UniProtKB: Actin-related protein 2/3 complex subunit 5 |
-分子 #7: Actin-related protein 2/3 complex subunit 1A
分子 | 名称: Actin-related protein 2/3 complex subunit 1A / タイプ: protein_or_peptide / ID: 7 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() |
分子量 | 理論値: 41.624262 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: MSLHQFLLEP ITCHAWNRDR TQIALSPNNH EVHIYKKNGS QWVKAHELKE HNGHITGIDW APKSDRIVTC GADRNAYVWS QKDGVWKPT LVILRINRAA TFVKWSPLEN KFAVGSGARL ISVCYFESEN DWWVSKHIKK PIRSTVLSLD WHPNNVLLAA G SCDFKCRV ...文字列: MSLHQFLLEP ITCHAWNRDR TQIALSPNNH EVHIYKKNGS QWVKAHELKE HNGHITGIDW APKSDRIVTC GADRNAYVWS QKDGVWKPT LVILRINRAA TFVKWSPLEN KFAVGSGARL ISVCYFESEN DWWVSKHIKK PIRSTVLSLD WHPNNVLLAA G SCDFKCRV FSAYIKEVDE KPASTPWGSK MPFGQLMSEF GGSGTGGWVH GVSFSASGSR LAWVSHDSTV SVADASKSVQ VS TLKTEFL PLLSVSFVSE NSVVAAGHDC CPMLFNYDDR GCLTFVSKLD IPKQSIQRNM SAMERFRNMD KRATTEDRNT ALE TLHQNS ITQVSIYEVD KQDCRKFCTT GIDGAMTIWD FKTLESSIQG LRIM UniProtKB: Actin-related protein 2/3 complex subunit 1A |
-分子 #8: ADENOSINE-5'-TRIPHOSPHATE
分子 | 名称: ADENOSINE-5'-TRIPHOSPHATE / タイプ: ligand / ID: 8 / コピー数: 2 / 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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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7 |
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凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI POLARA 300 |
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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 平均電子線量: 59.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD |
実験機器 | ![]() モデル: Tecnai Polara / 画像提供: FEI Company |
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画像解析
初期モデル | モデルのタイプ: PDB ENTRY PDBモデル - PDB ID: |
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最終 再構成 | 想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 4.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 130973 |
初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |