This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3rfa
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3rfa is ON HOLD Authors: Boal, A.K., Grove, T.L., McLaughlin, M.I., Yennawar, N., Booker, S.J., Rosenzweig, A.C. Description: X-ray structure of Rl...) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure of RlmN from Escherichia coli in complex with S-adenosylmethionine== | |
| + | <StructureSection load='3rfa' size='340' side='right'caption='[[3rfa]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3rfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFA FirstGlance]. <br> | ||
| + | </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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rf9|3rf9]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rlmN, yfgB, b2517, JW2501 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/23S_rRNA_(adenine(2503)-C(2))-methyltransferase 23S rRNA (adenine(2503)-C(2))-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.192 2.1.1.192] </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=3rfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfa OCA], [https://pdbe.org/3rfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfa RCSB], [https://www.ebi.ac.uk/pdbsum/3rfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfa ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/RLMN_ECOLI RLMN_ECOLI]] Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation.<ref>PMID:18025251</ref> <ref>PMID:21415317</ref> <ref>PMID:22891362</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The radical SAM (RS) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys 355) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys 355 is S-methylated and located proximal to the SAM methyl group, suggesting that SAM involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site. | ||
| - | + | Structural Basis for Methyl Transfer by a Radical SAM Enzyme.,Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC Science. 2011 Apr 28. PMID:21527678<ref>PMID:21527678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3rfa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ecoli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boal, A K]] | ||
| + | [[Category: Booker, S J]] | ||
| + | [[Category: Grove, T L]] | ||
| + | [[Category: McLaughlin, M I]] | ||
| + | [[Category: Rosenzweig, A C]] | ||
| + | [[Category: Yennawar, N]] | ||
| + | [[Category: Iron sulfur cluster]] | ||
| + | [[Category: Methyltransferase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Radical sam]] | ||
| + | [[Category: S-adenosylmethionine]] | ||
Current revision
X-ray structure of RlmN from Escherichia coli in complex with S-adenosylmethionine
| |||||||||||
