1i4j: Difference between revisions
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|GENE= RPL22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |GENE= RPL22 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1bxe|1BXE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4j OCA], [http://www.ebi.ac.uk/pdbsum/1i4j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i4j RCSB]</span> | |||
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[[Category: rna binding]] | [[Category: rna binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:30 2008'' | ||
Revision as of 21:14, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Gene: | RPL22 (Thermus thermophilus) | ||||||
| Related: | 1BXE
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF L22 RIBOSOMAL PROTEIN MUTANT
OverviewOverview
The ribosomal protein L22 is a core protein of the large ribosomal subunit interacting with all domains of the 23S rRNA. The triplet Met82-Lys83-Arg84 deletion in L22 from Escherichia coli renders cells resistant to erythromycin which is known as an inhibitor of the nascent peptide chain elongation. The crystal structure of the Thermus thermophilus L22 mutant with equivalent triplet Leu82-Lys83-Arg84 deletion has been determined at 1.8A resolution. The superpositions of the mutant and the wild-type L22 structures within the 50S subunits from Haloarcula marismortui and Deinococcus radiodurans show that the mutant beta-hairpin is bent inward the ribosome tunnel modifying the shape of its narrowest part and affecting the interaction between L22 and 23S rRNA. 23S rRNA nucleotides of domain V participating in erythromycin binding are located on the opposite sides of the tunnel and are brought to those positions by the interaction of the 23S rRNA with the L22 beta-hairpin. The mutation in the L22 beta-hairpin affects the orientation and distances between those nucleotides. This destabilizes the erythromycin-binding "pocket" formed by 23S rRNA nucleotides exposed at the tunnel surface. It seems that erythromycin, while still being able to interact with one side of the tunnel but not reaching the other, is therefore unable to block the polypeptide growth in the drug-resistant ribosome.
About this StructureAbout this Structure
1I4J is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin., Davydova N, Streltsov V, Wilce M, Liljas A, Garber M, J Mol Biol. 2002 Sep 20;322(3):635-44. PMID:12225755
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