2bcw
From Proteopedia
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| - | [[Image:2bcw.gif|left|200px]] | + | [[Image:2bcw.gif|left|200px]] |
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| - | '''Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex''' | + | {{Structure |
| + | |PDB= 2bcw |SIZE=350|CAPTION= <scene name='initialview01'>2bcw</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BCW is a [ | + | 2BCW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCW OCA]. |
==Reference== | ==Reference== | ||
| - | Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM., Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK, Mol Cell. 2005 Dec 9;20(5):723-31. PMID:[http:// | + | Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM., Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK, Mol Cell. 2005 Dec 9;20(5):723-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16337596 16337596] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome]] | [[Category: components involved in interaction between ef-g and l7/l12 stalk base of the ribosome]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:00:16 2008'' |
Revision as of 14:00, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Coordinates of the N-terminal domain of ribosomal protein L11,C-terminal domain of ribosomal protein L7/L12 and a portion of the G' domain of elongation factor G, as fitted into cryo-em map of an Escherichia coli 70S*EF-G*GDP*fusidic acid complex
Overview
During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC.
About this Structure
2BCW is a Protein complex structure of sequences from Escherichia coli, Thermotoga maritima and Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM., Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK, Mol Cell. 2005 Dec 9;20(5):723-31. PMID:16337596
Page seeded by OCA on Thu Mar 20 16:00:16 2008
