5hr7: Difference between revisions

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<StructureSection load='5hr7' size='340' side='right'caption='[[5hr7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5hr7' size='340' side='right'caption='[[5hr7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5hr7]] is a 4 chain structure with sequence from [http://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=5HR7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HR7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5hr7]] is a 4 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=5HR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HR7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.4&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <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">[[5hr6|5hr6]]</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=5hr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hr7 OCA], [https://pdbe.org/5hr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hr7 RCSB], [https://www.ebi.ac.uk/pdbsum/5hr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hr7 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rlmN, EcE24377A_2801 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/23S_rRNA_(adenine(2503)-C(2))-methyltransferase 23S rRNA (adenine(2503)-C(2))-methyltransferase], with EC number [http://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'>[http://proteopedia.org/fgij/fg.htm?mol=5hr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hr7 OCA], [http://pdbe.org/5hr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hr7 RCSB], [http://www.ebi.ac.uk/pdbsum/5hr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hr7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RLMN_ECO24 RLMN_ECO24]] 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.  
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boal, A K]]
[[Category: Boal AK]]
[[Category: Booker, S J]]
[[Category: Booker SJ]]
[[Category: Grove, T L]]
[[Category: Grove TL]]
[[Category: Schwalm, E L]]
[[Category: Schwalm EL]]
[[Category: Iron-sulfur cluster]]
[[Category: Oxidoreductase-rna complex]]
[[Category: Protein-rna complex]]
[[Category: Radical sam enzyme]]
[[Category: Transfer rna]]

Revision as of 13:51, 16 August 2023

X-ray crystal structure of C118A RlmN from Escherichia coli with cross-linked in vitro transcribed tRNAX-ray crystal structure of C118A RlmN from Escherichia coli with cross-linked in vitro transcribed tRNA

Structural highlights

5hr7 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

Publication Abstract from PubMed

RlmN is a dual-specificity RNA methylase that modifies C2 of adenosine 2503 (A2503) in 23S rRNA and C2 of adenosine 37 (A37) in several Escherichia coli transfer RNAs (tRNAs). A related methylase, Cfr, modifies C8 of A2503 via a similar mechanism, conferring resistance to multiple classes of antibiotics. Here, we report the x-ray structure of a key intermediate in the RlmN reaction, in which a Cys(118)-->Ala variant of the protein is cross-linked to a tRNA(Glu)substrate through the terminal methylene carbon of a formerly methylcysteinyl residue and C2 of A37. RlmN contacts the entire length of tRNA(Glu), accessing A37 by using an induced-fit strategy that completely unfolds the tRNA anticodon stem-loop, which is likely critical for recognition of both tRNA and ribosomal RNA substrates.

Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.,Schwalm EL, Grove TL, Booker SJ, Boal AK Science. 2016 Apr 15;352(6283):309-12. doi: 10.1126/science.aad5367. PMID:27081063[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Toh SM, Xiong L, Bae T, Mankin AS. The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. RNA. 2008 Jan;14(1):98-106. Epub 2007 Nov 19. PMID:18025251 doi:http://dx.doi.org/rna.814408
  2. Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science. 2011 Apr 29;332(6029):604-7. doi: 10.1126/science.1200877. Epub 2011 Mar, 17. PMID:21415317 doi:http://dx.doi.org/10.1126/science.1200877
  3. Benitez-Paez A, Villarroya M, Armengod ME. The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. RNA. 2012 Oct;18(10):1783-95. doi: 10.1261/rna.033266.112. Epub 2012 Aug 13. PMID:22891362 doi:http://dx.doi.org/10.1261/rna.033266.112
  4. Schwalm EL, Grove TL, Booker SJ, Boal AK. Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA. Science. 2016 Apr 15;352(6283):309-12. doi: 10.1126/science.aad5367. PMID:27081063 doi:http://dx.doi.org/10.1126/science.aad5367

5hr7, resolution 2.40Å

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