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| | <StructureSection load='5twk' size='340' side='right'caption='[[5twk]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5twk' size='340' side='right'caption='[[5twk]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5twk]] 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=5TWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TWK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5twk]] 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=5TWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TWK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5twj|5twj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rlmH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=5twk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5twk OCA], [https://pdbe.org/5twk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5twk RCSB], [https://www.ebi.ac.uk/pdbsum/5twk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5twk ProSAT]</span></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_(pseudouridine(1915)-N(3))-methyltransferase 23S rRNA (pseudouridine(1915)-N(3))-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.177 2.1.1.177] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5twk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5twk OCA], [http://pdbe.org/5twk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5twk RCSB], [http://www.ebi.ac.uk/pdbsum/5twk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5twk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RLMH_ECO45 RLMH_ECO45]] Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | + | [https://www.uniprot.org/uniprot/RLMH_ECOLI RLMH_ECOLI] Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes.<ref>PMID:18755835</ref> <ref>PMID:18755836</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: Beane, T J]] | + | [[Category: Beane TJ]] |
| - | [[Category: Koh, C S]] | + | [[Category: Koh CS]] |
| - | [[Category: Korostelev, A A]] | + | [[Category: Korostelev AA]] |
| - | [[Category: Madireddy, R]] | + | [[Category: Madireddy R]] |
| - | [[Category: Zamore, P D]] | + | [[Category: Zamore PD]] |
| - | [[Category: Helix 69]]
| + | |
| - | [[Category: Pseudouridine]]
| + | |
| - | [[Category: Rna methyltransferase]]
| + | |
| - | [[Category: Sinefungin]]
| + | |
| - | [[Category: Spout]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase-antibiotic complex]]
| + | |
| Structural highlights
Function
RLMH_ECOLI Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes.[1] [2]
Publication Abstract from PubMed
Eubacterial ribosomal large-subunit methyltransferase H (RlmH) methylates 23S ribosomal RNA pseudouridine 1915 (Psi1915), which lies near the ribosomal decoding center. The smallest member of the SPOUT superfamily of methyltransferases, RlmH lacks the RNA recognition domain found in larger methyltransferases. The catalytic mechanism of RlmH enzyme is unknown. Here, we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase inhibitor sinefungin. Our structural and biochemical studies reveal catalytically essential residues in the dimer-mediated asymmetrical active site. One monomer provides the SAM-binding site, whereas the conserved C-terminal tail of the second monomer provides residues essential for catalysis. Our findings elucidate the mechanism by which a small protein dimer assembles a functionally asymmetric architecture.
Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.,Koh CS, Madireddy R, Beane TJ, Zamore PD, Korostelev AA Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. PMID:28428565[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Purta E, Kaminska KH, Kasprzak JM, Bujnicki JM, Douthwaite S. YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA. RNA. 2008 Oct;14(10):2234-44. Epub 2008 Aug 28. PMID:18755835 doi:http://dx.doi.org/rna.1198108
- ↑ Ero R, Peil L, Liiv A, Remme J. Identification of pseudouridine methyltransferase in Escherichia coli. RNA. 2008 Oct;14(10):2223-33. Epub 2008 Aug 28. PMID:18755836 doi:http://dx.doi.org/rna.1186608
- ↑ Koh CS, Madireddy R, Beane TJ, Zamore PD, Korostelev AA. Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine. Sci Rep. 2017 Apr 20;7(1):969. doi: 10.1038/s41598-017-01186-5. PMID:28428565 doi:http://dx.doi.org/10.1038/s41598-017-01186-5
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