+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 6mrc | ||||||
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タイトル | ADP-bound human mitochondrial Hsp60-Hsp10 football complex | ||||||
要素 |
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キーワード | CHAPERONE / Complex / ADP / Football | ||||||
機能・相同性 | 機能・相同性情報 coated vesicle / isotype switching to IgG isotypes / mitochondrial unfolded protein response / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / apolipoprotein A-I binding / lipopolysaccharide receptor complex / protein import into mitochondrial intermembrane space / migrasome / high-density lipoprotein particle binding / positive regulation of T cell mediated immune response to tumor cell ...coated vesicle / isotype switching to IgG isotypes / mitochondrial unfolded protein response / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / apolipoprotein A-I binding / lipopolysaccharide receptor complex / protein import into mitochondrial intermembrane space / migrasome / high-density lipoprotein particle binding / positive regulation of T cell mediated immune response to tumor cell / Mitochondrial protein import / chaperonin ATPase / positive regulation of macrophage activation / cellular response to interleukin-7 / MyD88-dependent toll-like receptor signaling pathway / biological process involved in interaction with symbiont / 'de novo' protein folding / sperm plasma membrane / B cell proliferation / B cell activation / apolipoprotein binding / DNA replication origin binding / positive regulation of interferon-alpha production / apoptotic mitochondrial changes / protein maturation / positive regulation of interleukin-10 production / chaperone cofactor-dependent protein refolding / response to unfolded protein / RHOG GTPase cycle / chaperone-mediated protein complex assembly / clathrin-coated pit / sperm midpiece / protein folding chaperone / positive regulation of interleukin-12 production / Mitochondrial protein degradation / response to cold / T cell activation / secretory granule / isomerase activity / lipopolysaccharide binding / ATP-dependent protein folding chaperone / : / positive regulation of interleukin-6 production / osteoblast differentiation / positive regulation of type II interferon production / double-stranded RNA binding / positive regulation of T cell activation / unfolded protein binding / p53 binding / protein folding / single-stranded DNA binding / protein-folding chaperone binding / protein refolding / mitochondrial inner membrane / early endosome / protein stabilization / mitochondrial matrix / positive regulation of apoptotic process / ubiquitin protein ligase binding / negative regulation of apoptotic process / enzyme binding / cell surface / ATP hydrolysis activity / protein-containing complex / mitochondrion / RNA binding / extracellular space / extracellular exosome / ATP binding / membrane / metal ion binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
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: 3.08 Å | ||||||
データ登録者 | Gomez-Llorente, Y. / Jebara, F. / Patra, M. / Malik, R. / Nissemblat, S. / Azem, A. / Hirsch, J.A. / Ubarretxena-Belandia, I. | ||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Nat Commun / 年: 2020 タイトル: Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin. 著者: Yacob Gomez-Llorente / Fady Jebara / Malay Patra / Radhika Malik / Shahar Nisemblat / Orna Chomsky-Hecht / Avital Parnas / Abdussalam Azem / Joel A Hirsch / Iban Ubarretxena-Belandia / 要旨: mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES. Here we report the crystal structure of an ATP (ADP:BeF- ...mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins without the negative ATP binding inter-ring cooperativity of GroEL-GroES. Here we report the crystal structure of an ATP (ADP:BeF-bound) ground-state mimic double-ring mHsp60-(mHsp10) football complex, and the cryo-EM structures of the ADP-bound successor mHsp60-(mHsp10) complex, and a single-ring mHsp60-mHsp10 half-football. The structures explain the nucleotide dependence of mHsp60 ring formation, and reveal an inter-ring nucleotide symmetry consistent with the absence of negative cooperativity. In the ground-state a two-fold symmetric H-bond and a salt bridge stitch the double-rings together, whereas only the H-bond remains as the equatorial gap increases in an ADP football poised to split into half-footballs. Refolding assays demonstrate obligate single- and double-ring mHsp60 variants are active, and complementation analysis in bacteria shows the single-ring variant is as efficient as wild-type mHsp60. Our work provides a structural basis for active single- and double-ring complexes coexisting in the mHsp60-mHsp10 chaperonin reaction cycle. | ||||||
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 | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 6mrc.cif.gz | 1.4 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb6mrc.ent.gz | 1.2 MB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 6mrc.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 6mrc_validation.pdf.gz | 1.9 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 6mrc_full_validation.pdf.gz | 2.2 MB | 表示 | |
XML形式データ | 6mrc_validation.xml.gz | 254.4 KB | 表示 | |
CIF形式データ | 6mrc_validation.cif.gz | 367.8 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/mr/6mrc ftp://data.pdbj.org/pub/pdb/validation_reports/mr/6mrc | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
#1: タンパク質 | 分子量: 56263.559 Da / 分子数: 14 / 断片: UNP residues 27-552 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: HSPD1, HSP60 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P10809, EC: 3.6.4.9 #2: タンパク質 | 分子量: 10744.400 Da / 分子数: 14 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: HSPE1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P61604 #3: 化合物 | ChemComp-ADP / #4: 化合物 | ChemComp-MG / #5: 水 | ChemComp-HOH / | |
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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 |
-試料調製
構成要素 | 名称: Complex of Hsp60 with Hsp10 bound to ADP and Mg / タイプ: COMPLEX / Entity ID: #1-#2 / 由来: RECOMBINANT |
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分子量 | 値: 0.98 MDa / 実験値: NO |
由来(天然) | 生物種: Homo sapiens (ヒト) |
由来(組換発現) | 生物種: Escherichia coli (大腸菌) |
緩衝液 | pH: 7.7 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | グリッドの材料: GOLD / グリッドのタイプ: Homemade |
急速凍結 | 装置: HOMEMADE PLUNGER / 凍結剤: ETHANE |
-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: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / アライメント法: COMA FREE |
試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
撮影 | 平均露光時間: 10 sec. / 電子線照射量: 63 e/Å2 / 検出モード: COUNTING フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.13_2998: / 分類: 精密化 | ||||||||||||||||||||||||
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EMソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.08 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 66013 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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