+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 4v4w | |||||||||
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タイトル | Structure of a SecM-stalled E. coli ribosome complex obtained by fitting atomic models for RNA and protein components into cryo-EM map EMD-1143 | |||||||||
要素 |
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キーワード | RIBOSOME / SecM / nascent chain / signal transduction / RNA world / polypeptide exit tunnel / translocation / elongation arrest / protein-conducting channel | |||||||||
機能・相同性 | 機能・相同性情報 stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis ...stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / four-way junction DNA binding / translational termination / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / transcription elongation factor complex / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / protein homodimerization activity / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Escherichia coli (大腸菌) | |||||||||
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: 15 Å | |||||||||
データ登録者 | Mitra, K. / Frank, J. | |||||||||
引用 | ジャーナル: Mol Cell / 年: 2006 タイトル: Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements. 著者: Kakoli Mitra / Christiane Schaffitzel / Felcy Fabiola / Michael S Chapman / Nenad Ban / Joachim Frank / 要旨: In E. coli, the SecM nascent polypeptide causes elongation arrest, while interacting with 23S RNA bases A2058 and A749-753 in the exit tunnel of the large ribosomal subunit. We compared atomic models ...In E. coli, the SecM nascent polypeptide causes elongation arrest, while interacting with 23S RNA bases A2058 and A749-753 in the exit tunnel of the large ribosomal subunit. We compared atomic models fitted by real-space refinement into cryo-electron microscopy reconstructions of a pretranslocational and SecM-stalled E. coli ribosome complex. A cascade of RNA rearrangements propagates from the exit tunnel throughout the large subunit, affecting intersubunit bridges and tRNA positions, which in turn reorient small subunit RNA elements. Elongation arrest could result from the inhibition of mRNA.(tRNAs) translocation, E site tRNA egress, and perhaps translation factor activation at the GTPase-associated center. Our study suggests that the specific secondary and tertiary arrangement of ribosomal RNA provides the basis for internal signal transduction within the ribosome. Thus, the ribosome may itself have the ability to regulate its progression through translation by modulating its structure and consequently its receptivity to activation by cofactors. #1: ジャーナル: Nature / 年: 2005 タイトル: Structure of the E. coli protein-conducting channel bound to a translating ribosome 著者: Mitra, K. / Schaffitzel, C. / Shaikh, T. / Tama, F. / Jenni, S. / Brooks III, C.L. / Ban, N. / Frank, J. #2: ジャーナル: Cell(Cambridge,Mass.) / 年: 2003 タイトル: Locking and unlocking of ribosomal motions 著者: Valle, M. / Zavialov, A.V. / Sengupta, J. / Rawat, U. / Ehrenberg, M. / Frank, J. #3: ジャーナル: FEBS Lett / 年: 2006 タイトル: A model for co-translational translocation: ribosome-regulated nascent polypeptide translocation at the protein-conducting channel. 著者: Kakoli Mitra / Joachim Frank / 要旨: The protein-conducting channel (PCC) must allow both the translocation of soluble polypeptide regions across, and the lateral partitioning of hydrophobic transmembrane helices (TMHs) into, the ...The protein-conducting channel (PCC) must allow both the translocation of soluble polypeptide regions across, and the lateral partitioning of hydrophobic transmembrane helices (TMHs) into, the membrane. We have analyzed existing structures of ribosomes and ribosome-PCC complexes and observe conformational changes suggesting that the ribosome may sense and orient the nascent polypeptide and also facilitate conformational changes in the PCC, subsequently directing the nascent polypeptide into the appropriate PCC-mediated translocation mode. The PCC is predicted to be able to accommodate one central, consolidated channel or two segregated pores with different lipid accessibilities, which may enable the lipid-mediated partitioning of a TMH from one pore, while the other, aqueous, pore allows translocation of a hydrophilic polypeptide segment. Our hypothesis suggests a plausible mechanism for the transitioning of the PCC between different configurations. | |||||||||
履歴 |
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Remark 400 | COMPOUND THIS FILE, 2GYB, CONTAINS THE 30S SUBUNIT OF THE WHOLE RIBOSOMAL COMPLEX. THE ENTIRE CRYO- ...COMPOUND THIS FILE, 2GYB, CONTAINS THE 30S SUBUNIT OF THE WHOLE RIBOSOMAL COMPLEX. THE ENTIRE CRYO-EM STRUCTURE CONTAINS ONE 70S RIBOSOME AND ARE DEPOSITED UNDER 2GYB (30S SUBUNIT) AND 2GYC (50S SUBUNIT). | |||||||||
Remark 999 | SEQUENCE THIS PDB FILE WAS OBTAINED UPON RIGID BODY REFINEMENT OF A STARTING PDB FILE INTO A CRYO- ...SEQUENCE THIS PDB FILE WAS OBTAINED UPON RIGID BODY REFINEMENT OF A STARTING PDB FILE INTO A CRYO-EM MAP. THE E. COLI RIBOSOMES ARE OBTAINED NATURALLY, BUT FOR THE MODELING OF THE PROTEINS INTO THE EM MAP, AUTHORS SOMETIMES DID NOT MODEL IN THE ENTIRE PROTEIN. SOME RESIDUES ARE NOT WITHIN LINK DISTANCES FOR C-N BOND. |
-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 | 4v4w.cif.gz | 3 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb4v4w.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 4v4w.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 | 4v4w_validation.pdf.gz | 1.4 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 4v4w_full_validation.pdf.gz | 2.4 MB | 表示 | |
XML形式データ | 4v4w_validation.xml.gz | 346.4 KB | 表示 | |
CIF形式データ | 4v4w_validation.cif.gz | 529.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/v4/4v4w ftp://data.pdbj.org/pub/pdb/validation_reports/v4/4v4w | 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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-要素
-RNA鎖 , 4種, 6分子 AAAUAVAWB0B9
#1: RNA鎖 | 分子量: 482285.656 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) | ||||
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#2: RNA鎖 | 分子量: 24518.570 Da / 分子数: 3 / 由来タイプ: 天然 / 詳細: A-site, P-site, E-site / 由来: (天然) Escherichia coli (大腸菌) #22: RNA鎖 | | 分子量: 888503.500 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) #23: RNA鎖 | | 分子量: 34916.805 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) |
-30S ribosomal subunit protein ... , 19種, 19分子 ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASAT
#3: タンパク質 | 分子量: 26292.082 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7V0 |
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#4: タンパク質 | 分子量: 23078.785 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7V3 |
#5: タンパク質 | 分子量: 23311.924 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7V8 |
#6: タンパク質 | 分子量: 15618.051 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7W1 |
#7: タンパク質 | 分子量: 11181.867 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P02358 |
#8: タンパク質 | 分子量: 15384.665 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P02359 |
#9: タンパク質 | 分子量: 13857.205 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7W7 |
#10: タンパク質 | 分子量: 14440.777 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7X3 |
#11: タンパク質 | 分子量: 10996.753 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7R5 |
#12: タンパク質 | 分子量: 12388.068 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7R9 |
#13: タンパク質 | 分子量: 11245.101 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7S3 |
#14: タンパク質 | 分子量: 12738.911 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7S9 |
#15: タンパク質 | 分子量: 7117.352 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0AG59 |
#16: タンパク質 | 分子量: 9915.350 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0ADZ4 |
#17: タンパク質 | 分子量: 8822.135 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7T3 |
#18: タンパク質 | 分子量: 9134.767 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0AG63 |
#19: タンパク質 | 分子量: 8178.463 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7T7 |
#20: タンパク質 | 分子量: 9865.542 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7U3 |
#21: タンパク質 | 分子量: 9278.929 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) Escherichia coli (大腸菌) / 参照: UniProt: P0A7U7 |
+50S ribosomal protein ... , 26種, 27分子 B2B3B5BABBBCBDBEBFBGBHBIBJBKBLBMBNBOBQBRBSBTBUBWBXBZB1
-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 |
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