1eiz: Difference between revisions

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<StructureSection load='1eiz' size='340' side='right'caption='[[1eiz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1eiz' size='340' side='right'caption='[[1eiz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1eiz]] is a 1 chain structure with sequence from [https://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=1EIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1eiz]] is a 1 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=1EIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIZ 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></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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ej0|1ej0]]</div></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></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=1eiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eiz OCA], [https://pdbe.org/1eiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eiz RCSB], [https://www.ebi.ac.uk/pdbsum/1eiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eiz ProSAT]</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=1eiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eiz OCA], [https://pdbe.org/1eiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eiz RCSB], [https://www.ebi.ac.uk/pdbsum/1eiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eiz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RLME_ECOLI RLME_ECOLI]] Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.<ref>PMID:10748051</ref>
[https://www.uniprot.org/uniprot/RLME_ECOLI RLME_ECOLI] Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.<ref>PMID:10748051</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1eiz 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=1eiz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural, biochemical, and genetic techniques were applied to investigate the function of FtsJ, a recently identified heat shock protein. FtsJ is well conserved, from bacteria to humans. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. The molecular surface of FtsJ exposes a putative nucleic acid binding groove composed of highly conserved, positively charged residues. Substrate analysis showed that FtsJ methylates 23S rRNA within 50S ribosomal subunits in vitro and in vivo. Null mutations in ftsJ show a dramatically altered ribosome profile, a severe growth disadvantage, and a temperature-sensitive phenotype. Our results reveal an unexpected link between the heat shock response and RNA metabolism.
RNA methylation under heat shock control.,Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U Mol Cell. 2000 Aug;6(2):349-60. PMID:10983982<ref>PMID:10983982</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1eiz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bardwell, J C.A]]
[[Category: Bardwell JCA]]
[[Category: Bugl, H]]
[[Category: Bugl H]]
[[Category: Fauman, E B]]
[[Category: Fauman EB]]
[[Category: Jakob, U]]
[[Category: Jakob U]]
[[Category: Kushner, S R]]
[[Category: Kushner SR]]
[[Category: Saper, M A]]
[[Category: Saper MA]]
[[Category: Staker, B L]]
[[Category: Staker BL]]
[[Category: Zheng, F]]
[[Category: Zheng F]]
[[Category: 23s ribosomal rna]]
[[Category: Adenosyl methionine]]
[[Category: Adomet]]
[[Category: Ftsj]]
[[Category: Heat shock protein]]
[[Category: Methyltransferase]]
[[Category: Transferase]]
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