[日本語] English
万見
- EMDB-32823: Prefoldin-tubulin-TRiC complex -

+
データを開く


IDまたはキーワード:

読み込み中...

-
基本情報

登録情報
データベース: EMDB / ID: EMD-32823
タイトルPrefoldin-tubulin-TRiC complex
マップデータA differently local sharpened main map for the refinement
試料
  • 複合体: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
    • タンパク質・ペプチド: x 14種
  • リガンド: x 1種
キーワードchapronin complex / CHAPERONE
機能・相同性
機能・相同性情報


RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly ...RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / tubulin complex assembly / RPAP3/R2TP/prefoldin-like complex / BBSome-mediated cargo-targeting to cilium / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Formation of tubulin folding intermediates by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / RNA polymerase II core complex assembly / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-complex / negative regulation of amyloid fibril formation / protein folding chaperone complex / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / pericentriolar material / beta-tubulin binding / Association of TriC/CCT with target proteins during biosynthesis / microtubule-based process / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomerase activity / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / tubulin binding / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / response to virus / negative regulation of canonical Wnt signaling pathway / mRNA 5'-UTR binding / cilium / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / transcription corepressor activity / G-protein beta-subunit binding / azurophil granule lumen / unfolded protein binding / melanosome / protein folding / retina development in camera-type eye / amyloid-beta binding / protein-folding chaperone binding / cell body / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / cytoskeleton / protein stabilization / cadherin binding / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of DNA-templated transcription / Golgi apparatus / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol
類似検索 - 分子機能
Prefoldin subunit 3 / Prefoldin, subunit 4 / Prefoldin subunit 2 / Prefoldin beta-like / Prefoldin alpha-like / Prefoldin alpha subunit, archaea-type / Prefoldin subunit / Prefoldin subunit / Prefoldin / T-complex protein 1, alpha subunit ...Prefoldin subunit 3 / Prefoldin, subunit 4 / Prefoldin subunit 2 / Prefoldin beta-like / Prefoldin alpha-like / Prefoldin alpha subunit, archaea-type / Prefoldin subunit / Prefoldin subunit / Prefoldin / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family
類似検索 - ドメイン・相同性
Prefoldin subunit 6 / Prefoldin subunit 1 / T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / Prefoldin subunit 3 / T-complex protein 1 subunit beta ...Prefoldin subunit 6 / Prefoldin subunit 1 / T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / Prefoldin subunit 3 / T-complex protein 1 subunit beta / Prefoldin subunit 5 / T-complex protein 1 subunit eta / Prefoldin subunit 4 / Prefoldin subunit 2
類似検索 - 構成要素
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: 3.85 Å
データ登録者Roh SH / Park J
資金援助 韓国, 1件
OrganizationGrant number国
National Research Foundation (NRF, Korea) 韓国
引用ジャーナル: Cell / 年: 2022
タイトル: Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.
著者: Daniel Gestaut / Yanyan Zhao / Junsun Park / Boxue Ma / Alexander Leitner / Miranda Collier / Grigore Pintilie / Soung-Hun Roh / Wah Chiu / Judith Frydman /
要旨: The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of ...The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human prefoldin and TRiC. We find unstructured β-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded β-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates.
履歴
登録2022年2月7日-
ヘッダ(付随情報) 公開2022年12月21日-
マップ公開2022年12月21日-
更新2024年6月26日-
現状2024年6月26日処理サイト: PDBj / 状態: 公開

-
構造の表示

添付画像

emd_32823.png

ダウンロードとリンク

-
マップ

ファイルダウンロード / ファイル: emd_32823.map.gz / 形式: CCP4 / 大きさ: 125 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈A differently local sharpened main map for the refinement
ボクセルのサイズX=Y=Z: 1.02 Å
密度
表面レベル登録者による: 0.943
最小 - 最大-7.622423 - 11.117316000000001
平均 (標準偏差)0.019353984 (±0.24627073)
対称性空間群: 1
詳細

EMDB XML:

マップ形状
Axis orderXYZ
Origin000
サイズ320320320
Spacing320320320
セルA=B=C: 326.4 Å
α=β=γ: 90.0 °

-
添付データ

-
追加マップ: A B-factor sharpened map

ファイルemd_32823_additional_1.map
注釈A B-factor sharpened map
投影像・断面図
軸ZYX

投影像

断面 (1/2)
密度ヒストグラム

ヒストグラム

ヒストグラム (対数)

-
ハーフマップ: A half map

ファイルemd_32823_half_map_1.map
注釈A half map
投影像・断面図
軸ZYX

投影像

断面 (1/2)
密度ヒストグラム

ヒストグラム

ヒストグラム (対数)

-
ハーフマップ: A half map

ファイルemd_32823_half_map_2.map
注釈A half map
投影像・断面図
軸ZYX

投影像

断面 (1/2)
密度ヒストグラム

ヒストグラム

ヒストグラム (対数)

-
試料の構成要素

+
全体 : Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex

全体名称: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
要素
  • 複合体: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
    • タンパク質・ペプチド: Prefoldin subunit 1
    • タンパク質・ペプチド: Prefoldin subunit 2
    • タンパク質・ペプチド: Prefoldin subunit 3
    • タンパク質・ペプチド: Prefoldin subunit 4
    • タンパク質・ペプチド: Prefoldin subunit 5
    • タンパク質・ペプチド: Prefoldin subunit 6
    • タンパク質・ペプチド: T-complex protein 1 subunit alpha
    • タンパク質・ペプチド: T-complex protein 1 subunit beta
    • タンパク質・ペプチド: T-complex protein 1 subunit gamma
    • タンパク質・ペプチド: T-complex protein 1 subunit delta
    • タンパク質・ペプチド: T-complex protein 1 subunit epsilon
    • タンパク質・ペプチド: T-complex protein 1 subunit zeta
    • タンパク質・ペプチド: T-complex protein 1 subunit eta
    • タンパク質・ペプチド: T-complex protein 1 subunit theta
  • リガンド: ADENOSINE-5'-DIPHOSPHATE

+
超分子 #1: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex

超分子名称: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#14
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 1 MDa

+
分子 #1: Prefoldin subunit 1

分子名称: Prefoldin subunit 1 / タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 14.234497 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列:
MAAPVDLELK KAFTELQAKV IDTQQKVKLA DIQIEQLNRT KKHAHLTDTE IMTLVDETNM YEGVGRMFIL QSKEAIHSQL LEKQKIAEE KIKELEQKKS YLERSVKEAE DNIREMLMAR RAQ

UniProtKB: Prefoldin subunit 1

+
分子 #2: Prefoldin subunit 2

分子名称: Prefoldin subunit 2 / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 16.67283 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列:
MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPA LENNKEQIQK IIETLTQQLQ AKGKELNEFR EKHNIRLMGE DEKPAAKENS EGAGAKASSA GVLVS

UniProtKB: Prefoldin subunit 2

+
分子 #3: Prefoldin subunit 3

分子名称: Prefoldin subunit 3 / タイプ: protein_or_peptide / ID: 3 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 22.65893 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列: MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY KFMELNLAQK KRRLKGQIPE IKQTLEILK YMQKKKESTN SMETRFLLAD NLYCKASVPP TDKVCLWLGA NVMLEYDIDE AQALLEKNLS TATKNLDSLE E DLDFLRDQ ...文字列:
MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY KFMELNLAQK KRRLKGQIPE IKQTLEILK YMQKKKESTN SMETRFLLAD NLYCKASVPP TDKVCLWLGA NVMLEYDIDE AQALLEKNLS TATKNLDSLE E DLDFLRDQ FTTTEVNMAR VYNWDVKRRN KDDSTKNKA

UniProtKB: Prefoldin subunit 3

+
分子 #4: Prefoldin subunit 4

分子名称: Prefoldin subunit 4 / タイプ: protein_or_peptide / ID: 4 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 16.160071 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列:
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA DDDCLMIPYQ IGDVFISHSQ EETQEMLEE AKKNLQEEID ALESRVESIQ RVLADLKVQL YAKFGSNINL EADESHHHHH H

UniProtKB: Prefoldin subunit 4

+
分子 #5: Prefoldin subunit 5

分子名称: Prefoldin subunit 5 / タイプ: protein_or_peptide / ID: 5 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 16.051647 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列:
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTG YYVEKTAEDA KDFFKRKIDF LTKQMEKIQP ALQEKHAMKQ AVMEMMSQKI Q

UniProtKB: Prefoldin subunit 5

+
分子 #6: Prefoldin subunit 6

分子名称: Prefoldin subunit 6 / タイプ: protein_or_peptide / ID: 6 / コピー数: 1 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 14.603641 KDa
組換発現生物種: Trichoplusia ni (イラクサキンウワバ)
配列文字列:
MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKR YESQLRDLER QSEQQRETLA QLQQEFQRAQ AAKAGAPGKA

UniProtKB: Prefoldin subunit 6

+
分子 #7: T-complex protein 1 subunit alpha

分子名称: T-complex protein 1 subunit alpha / タイプ: protein_or_peptide / ID: 7 / コピー数: 2 / 光学異性体: LEVO
由来(天然)生物種: Homo sapiens (ヒト)
分子量理論値: 60.418477 KDa
組換発現生物種: