|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==T. thermophilus 16S rRNA G527 methyltransferase in complex with AdoMet and AMP in space group P61== | | ==T. thermophilus 16S rRNA G527 methyltransferase in complex with AdoMet and AMP in space group P61== |
| - | <StructureSection load='3g89' size='340' side='right' caption='[[3g89]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3g89' size='340' side='right'caption='[[3g89]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g89]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G89 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g89]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G89 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g88|3g88]], [[3g8a|3g8a]], [[3g8b|3g8b]]</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=3g89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g89 OCA], [https://pdbe.org/3g89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g89 RCSB], [https://www.ebi.ac.uk/pdbsum/3g89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g89 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gidB, rsmG, TTHA1971 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=3g89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g89 OCA], [http://pdbe.org/3g89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g89 RCSB], [http://www.ebi.ac.uk/pdbsum/3g89 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g89 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RSMG_THET8 RSMG_THET8]] Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate.[HAMAP-Rule:MF_00074]<ref>PMID:19622680</ref> | + | [https://www.uniprot.org/uniprot/RSMG_THET8 RSMG_THET8] Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate.[HAMAP-Rule:MF_00074]<ref>PMID:19622680</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/3g89_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/3g89_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 35: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thet8]] | + | [[Category: Large Structures]] |
| - | [[Category: Belardinelli, R]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Dahlberg, A E]] | + | [[Category: Belardinelli R]] |
| - | [[Category: Demirci, H]] | + | [[Category: Dahlberg AE]] |
| - | [[Category: Gregory, S T]] | + | [[Category: Demirci H]] |
| - | [[Category: Gualerzi, C]] | + | [[Category: Gregory ST]] |
| - | [[Category: Jogl, G]] | + | [[Category: Gualerzi C]] |
| - | [[Category: 16s rrna methyltransferase]]
| + | [[Category: Jogl G]] |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Rrna processing]]
| + | |
| - | [[Category: S-adenosyl-l-methionine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
RSMG_THET8 Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate.[HAMAP-Rule:MF_00074][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The RsmG methyltransferase is responsible for N(7) methylation of G527 of 16S rRNA in bacteria. Here, we report the identification of the Thermus thermophilus rsmG gene, the isolation of rsmG mutants, and the solution of RsmG X-ray crystal structures at up to 1.5 A resolution. Like their counterparts in other species, T. thermophilus rsmG mutants are weakly resistant to the aminoglycoside antibiotic streptomycin. Growth competition experiments indicate a physiological cost to loss of RsmG activity, consistent with the conservation of the modification site in the decoding region of the ribosome. In contrast to Escherichia coli RsmG, which has been reported to recognize only intact 30S subunits, T. thermophilus RsmG shows no in vitro methylation activity against native 30S subunits, only low activity with 30S subunits at low magnesium concentration, and maximum activity with deproteinized 16S rRNA. Cofactor-bound crystal structures of RsmG reveal a positively charged surface area remote from the active site that binds an adenosine monophosphate molecule. We conclude that an early assembly intermediate is the most likely candidate for the biological substrate of RsmG.
Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.,Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G RNA. 2009 Sep;15(9):1693-704. Epub 2009 Jul 21. PMID:19622680[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G. Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. RNA. 2009 Sep;15(9):1693-704. Epub 2009 Jul 21. PMID:19622680 doi:10.1261/rna.1652709
- ↑ Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G. Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. RNA. 2009 Sep;15(9):1693-704. Epub 2009 Jul 21. PMID:19622680 doi:10.1261/rna.1652709
|
