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- PDB-1zo1: IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiati... -
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Basic information
Entry | Database: PDB / ID: 1zo1 | ||||||
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Title | IF2, IF1, and tRNA fitted to cryo-EM data OF E. COLI 70S initiation complex | ||||||
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![]() | translation/RNA / E. COLI / RIBOSOME / INITIATION OF PROTEIN SYNTHESIS / INITIATION FACTOR / CRYO-ELETRON MICROSCOPY / translation-RNA COMPLEX | ||||||
Function / homology | ![]() guanosine tetraphosphate binding / ribosomal small subunit binding / chaperone-mediated protein folding / translational initiation / translation initiation factor activity / response to cold / ribosome binding / rRNA binding / GTPase activity / GTP binding ...guanosine tetraphosphate binding / ribosomal small subunit binding / chaperone-mediated protein folding / translational initiation / translation initiation factor activity / response to cold / ribosome binding / rRNA binding / GTPase activity / GTP binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 13.8 Å | ||||||
![]() | Allen, G.S. / Zavialov, A. / Gursky, R. / Ehrenberg, M. / Frank, J. | ||||||
![]() | ![]() Title: The cryo-EM structure of a translation initiation complex from Escherichia coli. Authors: Gregory S Allen / Andrey Zavialov / Richard Gursky / Måns Ehrenberg / Joachim Frank / ![]() Abstract: The 70S ribosome and its complement of factors required for initiation of translation in E. coli were purified separately and reassembled in vitro with GDPNP, producing a stable initiation complex ...The 70S ribosome and its complement of factors required for initiation of translation in E. coli were purified separately and reassembled in vitro with GDPNP, producing a stable initiation complex (IC) stalled after 70S assembly. We have obtained a cryo-EM reconstruction of the IC showing IF2*GDPNP at the intersubunit cleft of the 70S ribosome. IF2*GDPNP contacts the 30S and 50S subunits as well as fMet-tRNA(fMet). IF2 here adopts a conformation radically different from that seen in the recent crystal structure of IF2. The C-terminal domain of IF2 binds to the single-stranded portion of fMet-tRNA(fMet), thereby forcing the tRNA into a novel orientation at the P site. The GTP binding domain of IF2 binds to the GTPase-associated center of the 50S subunit in a manner similar to EF-G and EF-Tu. Additionally, we present evidence for the localization of IF1, IF3, one C-terminal domain of L7/L12, and the N-terminal domain of IF2 in the initiation complex. | ||||||
History |
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Structure visualization
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PDBx/mmCIF format | ![]() | 158.5 KB | Display | ![]() |
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PDB format | ![]() | 103.6 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 648.9 KB | Display | ![]() |
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Full document | ![]() | 768.2 KB | Display | |
Data in XML | ![]() | 33.5 KB | Display | |
Data in CIF | ![]() | 50.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1248MC ![]() 1249MC ![]() 1zo3C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Components
#1: RNA chain | Mass: 24518.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 54209.820 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 8116.468 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: |