- EMDB-2448: Cryo-EM structure of T. thermophilus 30S Translation Initiation c... -
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IDまたはキーワード:
読み込み中...
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基本情報
登録情報
データベース: EMDB / ID: EMD-2448
タイトル
Cryo-EM structure of T. thermophilus 30S Translation Initiation complex
マップデータ
Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2.
試料
試料: Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2.
ジャーナル: Proc Natl Acad Sci U S A / 年: 2013 タイトル: Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. 著者: Angelita Simonetti / Stefano Marzi / Isabelle M L Billas / Albert Tsai / Attilio Fabbretti / Alexander G Myasnikov / Pierre Roblin / Andrea C Vaiana / Isabelle Hazemann / Daniel Eiler / ...著者: Angelita Simonetti / Stefano Marzi / Isabelle M L Billas / Albert Tsai / Attilio Fabbretti / Alexander G Myasnikov / Pierre Roblin / Andrea C Vaiana / Isabelle Hazemann / Daniel Eiler / Thomas A Steitz / Joseph D Puglisi / Claudio O Gualerzi / Bruno P Klaholz / 要旨: Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle ...Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC, it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl(fMet)-tRNA(fMet) positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.
ダウンロード / ファイル: emd_2448.map.gz / 形式: CCP4 / 大きさ: 33.5 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈
Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2.
ボクセルのサイズ
X=Y=Z: 1.82 Å
密度
表面レベル
登録者による: 0.169 / ムービー #1: 0.169
最小 - 最大
-0.76591331 - 3.60590792
平均 (標準偏差)
0.0375132 (±0.22922359)
対称性
空間群: 1
詳細
EMDB XML:
マップ形状
Axis order
X
Y
Z
Origin
-103
-104
-104
サイズ
208
208
208
Spacing
208
208
208
セル
A=B=C: 378.56 Å α=β=γ: 90.0 °
CCP4マップ ヘッダ情報:
mode
Image stored as Reals
Å/pix. X/Y/Z
1.82
1.82
1.82
M x/y/z
208
208
208
origin x/y/z
0.000
0.000
0.000
length x/y/z
378.560
378.560
378.560
α/β/γ
90.000
90.000
90.000
start NX/NY/NZ
0
0
-40
NX/NY/NZ
55
55
81
MAP C/R/S
1
2
3
start NC/NR/NS
-104
-103
-104
NC/NR/NS
208
208
208
D min/max/mean
-0.766
3.606
0.038
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添付データ
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試料の構成要素
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全体 : Bacterial 30S Translation Initiation complex from T. thermophilus...
全体
名称: Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2.
要素
試料: Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2.
複合体: 30S
タンパク質・ペプチド: Translation Initiation Factor 1
タンパク質・ペプチド: Translation Initiation Factor 2
RNA: mRNA
RNA: fMet-tRNA
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超分子 #1000: Bacterial 30S Translation Initiation complex from T. thermophilus...
超分子
名称: Bacterial 30S Translation Initiation complex from T. thermophilus containing 30S, IF1, IF2, mRNA and fMet-tRNA. The structure have been used for modeling full atom IF2. タイプ: sample / ID: 1000 / 集合状態: monomer / Number unique components: 5
Particle selection was done semiautomatically with the BOXER routine of the EMAN2 software package followed by visual inspection. Defocus value estimation and contrast transfer function (CTF) correction by phase flipping were done using the program CTFIT from the EMAN2. Sample homogeneity was tested through 3D resampling and classification (3D-SC) using the IMAGIC suite, and structure determination and refinement were done using the EMAN2 software package.
CTF補正
詳細: Each particle
最終 再構成
想定した対称性 - 点群: C1 (非対称) / アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 11.5 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: EMAN2, IMAGIC / 使用した粒子像数: 13000