3fzg

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Current revision (08:25, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3fzg' size='340' side='right'caption='[[3fzg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3fzg' size='340' side='right'caption='[[3fzg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3fzg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FZG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3fzg]] 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=3FZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FZG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3frh|3frh]], [[3fri|3fri]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">armA, pMUR050_016 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fzg OCA], [https://pdbe.org/3fzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fzg RCSB], [https://www.ebi.ac.uk/pdbsum/3fzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fzg 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=3fzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fzg OCA], [https://pdbe.org/3fzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fzg RCSB], [https://www.ebi.ac.uk/pdbsum/3fzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fzg ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q6F5A0_ECOLX Q6F5A0_ECOLX]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fzg ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fzg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Aminoglycosides 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.
 
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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<ref>PMID:19303884</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3fzg" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Courvalin, P]]
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[[Category: Courvalin P]]
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[[Category: Galimand, M]]
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[[Category: Galimand M]]
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[[Category: Mechulam, Y]]
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[[Category: Mechulam Y]]
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[[Category: Panvert, M]]
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[[Category: Panvert M]]
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[[Category: Schmitt, E]]
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[[Category: Schmitt E]]
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[[Category: Methyltransferase]]
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[[Category: Plasmid]]
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[[Category: Transferase]]
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Current revision

Structure of the 16S rRNA methylase ArmA

PDB ID 3fzg

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