2b3t
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= hemK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), prfA, sueB, uar ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= hemK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), prfA, sueB, uar ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ml5|1ML5]], [[1gqe|1GQE]], [[1nv8|1NV8]], [[1t43|1T43]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3t OCA], [http://www.ebi.ac.uk/pdbsum/2b3t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b3t RCSB]</span> | ||
}} | }} | ||
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[[Category: Tilbeurgh, H van.]] | [[Category: Tilbeurgh, H van.]] | ||
[[Category: Ulryck, N.]] | [[Category: Ulryck, N.]] | ||
| - | [[Category: | + | [[Category: conformational change]] |
| - | [[Category: release factor | + | [[Category: methylation]] |
| + | [[Category: release factor]] | ||
| + | [[Category: translation termination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:01:03 2008'' |
Revision as of 23:01, 30 March 2008
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| , resolution 3.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | hemK (Escherichia coli), prfA, sueB, uar (Escherichia coli) | ||||||
| Related: | 1ML5, 1GQE, 1NV8, 1T43
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Molecular basis for bacterial class 1 release factor methylation by PrmC
Overview
Class I release factors bind to ribosomes in response to stop codons and trigger peptidyl-tRNA hydrolysis at the P site. Prokaryotic and eukaryotic RFs share one motif: a GGQ tripeptide positioned in a loop at the end of a stem region that interacts with the ribosomal peptidyl transferase center. The glutamine side chain of this motif is specifically methylated in both prokaryotes and eukaryotes. Methylation in E. coli is due to PrmC and results in strong stimulation of peptide chain release. We have solved the crystal structure of the complex between E. coli RF1 and PrmC bound to the methyl donor product AdoHCy. Both the GGQ domain (domain 3) and the central region (domains 2 and 4) of RF1 interact with PrmC. Structural and mutagenic data indicate a compact conformation of RF1 that is unlike its conformation when it is bound to the ribosome but is similar to the crystal structure of the protein alone.
About this Structure
2B3T is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Molecular basis for bacterial class I release factor methylation by PrmC., Graille M, Heurgue-Hamard V, Champ S, Mora L, Scrima N, Ulryck N, van Tilbeurgh H, Buckingham RH, Mol Cell. 2005 Dec 22;20(6):917-27. PMID:16364916
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