3g89 | pdb_00003g89

T. thermophilus 16S rRNA G527 methyltransferase in complex with AdoMet and AMP in space group P61

spinqualitylabelsall models 3g89, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g89 is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: AMP, HIC, SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RSMG_THET8 Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate.[HAMAP-Rule:MF_00074] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The RsmG methyltransferase is responsible for N(7) methylation of G527 of 16S rRNA in bacteria. Here, we report the identification of the Thermus thermophilus rsmG gene, the isolation of rsmG mutants, and the solution of RsmG X-ray crystal structures at up to 1.5 A resolution. Like their counterparts in other species, T. thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome. In contrast to Escherichia coli RsmG, which has been reported to recognize only intact 30S subunits, T. thermophilus RsmG shows no in vitro methylation activity against native 30S subunits, only low activity with 30S subunits at low magnesium concentration, and maximum activity with deproteinized 16S rRNA. Cofactor-bound crystal structures of RsmG reveal a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule. We conclude that an early assembly intermediate is the most likely candidate for the biological substrate of RsmG. Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.,Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G RNA. 2009 Sep;15(9):1693-704. Epub 2009 Jul 21. PMID:19622680 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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