1gz0: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gz0 OCA], [https://pdbe.org/1gz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gz0 ProSAT], [https://www.topsan.org/Proteins/BSGI/1gz0 TOPSAN]</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=1gz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gz0 OCA], [https://pdbe.org/1gz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gz0 ProSAT], [https://www.topsan.org/Proteins/BSGI/1gz0 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/1gz0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/1gz0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <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> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gz0 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gz0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Escherichia coli, RlmB catalyzes the methylation of guanosine 2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. The crystal structure of this 2'O-methyltransferase has been determined at 2.5 A resolution. RlmB consists of an N-terminal domain connected by a flexible extended linker to a catalytic C-terminal domain and forms a dimer in solution. The C-terminal domain displays a divergent methyltransferase fold with a unique knotted region, and lacks the classic AdoMet binding site features. The N-terminal domain is similar to ribosomal proteins L7 and L30, suggesting a role in 23S rRNA recognition. The conserved residues in this novel family of 2'O-methyltransferases cluster in the knotted region, suggesting the location of the catalytic and AdoMet binding sites. | |||
The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot.,Michel G, Sauve V, Larocque R, Li Y, Matte A, Cygler M Structure. 2002 Oct;10(10):1303-15. PMID:12377117<ref>PMID:12377117</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1gz0" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 03:01, 21 November 2024
23S RIBOSOMAL RNA G2251 2'O-METHYLTRANSFERASE RLMB23S RIBOSOMAL RNA G2251 2'O-METHYLTRANSFERASE RLMB
Structural highlights
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 PubMedIn Escherichia coli, RlmB catalyzes the methylation of guanosine 2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. The crystal structure of this 2'O-methyltransferase has been determined at 2.5 A resolution. RlmB consists of an N-terminal domain connected by a flexible extended linker to a catalytic C-terminal domain and forms a dimer in solution. The C-terminal domain displays a divergent methyltransferase fold with a unique knotted region, and lacks the classic AdoMet binding site features. The N-terminal domain is similar to ribosomal proteins L7 and L30, suggesting a role in 23S rRNA recognition. The conserved residues in this novel family of 2'O-methyltransferases cluster in the knotted region, suggesting the location of the catalytic and AdoMet binding sites. The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot.,Michel G, Sauve V, Larocque R, Li Y, Matte A, Cygler M Structure. 2002 Oct;10(10):1303-15. PMID:12377117[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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