1gqe
From Proteopedia
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- | [[Image:1gqe.gif|left|200px]] | + | [[Image:1gqe.gif|left|200px]] |
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- | '''POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM ESCHERICHIA COLI''' | + | {{Structure |
+ | |PDB= 1gqe |SIZE=350|CAPTION= <scene name='initialview01'>1gqe</scene>, resolution 1.81Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM ESCHERICHIA COLI''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1GQE is a [ | + | 1GQE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQE OCA]. |
==Reference== | ==Reference== | ||
- | Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1., Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M, Mol Cell. 2001 Dec;8(6):1375-82. PMID:[http:// | + | Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1., Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M, Mol Cell. 2001 Dec;8(6):1375-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11779511 11779511] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: translation]] | [[Category: translation]] | ||
- | ''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 11:26:35 2008'' |
Revision as of 09:26, 20 March 2008
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, resolution 1.81Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
POLYPEPTIDE CHAIN RELEASE FACTOR 2 (RF2) FROM ESCHERICHIA COLI
Overview
Bacterial release factor RF2 promotes termination of protein synthesis, specifically recognizing stop codons UAA or UGA. The crystal structure of Escherichia coli RF2 has been determined to a resolution of 1.8 A. RF2 is structurally distinct from its eukaryotic counterpart eRF1. The tripeptide SPF motif, thought to confer RF2 stop codon specificity, and the universally conserved GGQ motif, proposed to be involved with the peptidyl transferase center, are exposed in loops only 23 A apart, and the structure suggests that stop signal recognition is more complex than generally believed.
About this Structure
1GQE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1., Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M, Mol Cell. 2001 Dec;8(6):1375-82. PMID:11779511
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