4rx1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rx1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorangium_cellulosum Sorangium cellulosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RX1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rx1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorangium_cellulosum Sorangium cellulosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RX1 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.472Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</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=4rx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx1 OCA], [https://pdbe.org/4rx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rx1 RCSB], [https://www.ebi.ac.uk/pdbsum/4rx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rx1 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=4rx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx1 OCA], [https://pdbe.org/4rx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rx1 RCSB], [https://www.ebi.ac.uk/pdbsum/4rx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rx1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/B2L3G9_SORCE B2L3G9_SORCE] | [https://www.uniprot.org/uniprot/B2L3G9_SORCE B2L3G9_SORCE] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Methylation of bacterial 16S rRNA within the ribosomal decoding center confers exceptionally high resistance to aminoglycoside antibiotics. This resistance mechanism is exploited by aminoglycoside producers for self-protection while functionally equivalent methyltransferases have been acquired by human and animal pathogenic bacteria. Here, we report structural and functional analyses of the Sorangium cellulosum So ce56 aminoglycoside resistance-conferring methyltransferase Kmr. Our results demonstrate that Kmr is a 16S rRNA methyltransferase acting at residue A1408 to confer a canonical aminoglycoside resistance spectrum in Escherichia coli. Kmr possesses a class I methyltransferase core fold but with dramatic differences in the regions which augment this structure to confer substrate specificity in functionally related enzymes. Most strikingly, the region linking core beta-strands 6 and 7, which forms part of the S-adenosyl-l-methionine (SAM) binding pocket and contributes to base flipping by the m(1)A1408 methyltransferase NpmA, is disordered in Kmr, correlating with an exceptionally weak affinity for SAM. Kmr is unexpectedly insensitive to substitutions of residues critical for activity of other 16S rRNA (A1408) methyltransferases and also to the effects of by-product inhibition by S-adenosylhomocysteine (SAH). Collectively, our results indicate that adoption of a catalytically competent Kmr conformation and binding of the obligatory cosubstrate SAM must be induced by interaction with the 30S subunit substrate. | ||
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| - | 30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr.,Savic M, Sunita S, Zelinskaya N, Desai PM, Macmaster R, Vinal K, Conn GL Antimicrob Agents Chemother. 2015 May;59(5):2807-16. doi: 10.1128/AAC.00056-15., Epub 2015 Mar 2. PMID:25733511<ref>PMID:25733511</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4rx1" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal Structure of antibiotic-resistance methyltransferase Kmr
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