3fri: Difference between revisions
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<StructureSection load='3fri' size='340' side='right'caption='[[3fri]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3fri' size='340' side='right'caption='[[3fri]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3fri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FRI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fri OCA], [https://pdbe.org/3fri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fri RCSB], [https://www.ebi.ac.uk/pdbsum/3fri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fri ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fri OCA], [https://pdbe.org/3fri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fri RCSB], [https://www.ebi.ac.uk/pdbsum/3fri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fri ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q763K9_ECOLX Q763K9_ECOLX] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Courvalin | [[Category: Courvalin P]] | ||
[[Category: Dupechez | [[Category: Dupechez M]] | ||
[[Category: Galimand | [[Category: Galimand M]] | ||
[[Category: Mechulam | [[Category: Mechulam Y]] | ||
[[Category: Panvert | [[Category: Panvert M]] | ||
[[Category: Schmitt | [[Category: Schmitt E]] | ||
Latest revision as of 18:31, 1 November 2023
Structure of the 16S rRNA methylase RmtB, I222Structure of the 16S rRNA methylase RmtB, I222
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAminoglycosides are used extensively for the treatment of severe infections due to Gram-negative bacteria. However, certain species have become highly resistant after acquisition of genes for methyltransferases which catalyze post-transcriptional methylation of N7-G1405 in 16 S rRNA of 30 S ribosomal subunits. Inactivation of this enzymatic activity is therefore an important challenge for development of an effective therapy. The present work describes the crystallographic structures of methyltransferases RmtB and ArmA from clinical isolates. Together with biochemical experiments, the 3D structures indicate that the N-terminal domain specific for this family of methyltransferases is required for enzymatic activity. Site-directed mutagenesis has enabled important residues for catalysis and RNA binding to be identified. These high-resolution structures should underpin the design of potential inhibitors of these enzymes, which could be used to restore the activity of aminoglycosides against resistant pathogens. Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases.,Schmitt E, Galimand M, Panvert M, Courvalin P, Mechulam Y J Mol Biol. 2009 May 8;388(3):570-82. Epub 2009 Mar 20. PMID:19303884[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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