3ces: Difference between revisions

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<StructureSection load='3ces' size='340' side='right'caption='[[3ces]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
<StructureSection load='3ces' size='340' side='right'caption='[[3ces]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ces]] is a 4 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=3CES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CES FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ces]] 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=3CES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CES FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gidA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.412&#8491;</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=3ces FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ces OCA], [https://pdbe.org/3ces PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ces RCSB], [https://www.ebi.ac.uk/pdbsum/3ces PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ces 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=3ces FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ces OCA], [https://pdbe.org/3ces PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ces RCSB], [https://www.ebi.ac.uk/pdbsum/3ces PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ces ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MNMG_ECOLI MNMG_ECOLI]] NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.<ref>PMID:11544186</ref> <ref>PMID:17062623</ref> <ref>PMID:9603884</ref>
[https://www.uniprot.org/uniprot/MNMG_ECOLI MNMG_ECOLI] NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.<ref>PMID:11544186</ref> <ref>PMID:17062623</ref> <ref>PMID:9603884</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=3ces 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=3ces ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.
Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.,Shi R, Villarroya M, Ruiz-Partida R, Li Y, Proteau A, Prado S, Moukadiri I, Benitez-Paez A, Lomas R, Wagner J, Matte A, Velazquez-Campoy A, Armengod ME, Cygler M J Bacteriol. 2009 Dec;191(24):7614-9. Epub 2009 Oct 2. PMID:19801413<ref>PMID:19801413</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ces" 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: Structural genomic]]
[[Category: Cygler M]]
[[Category: Cygler, M]]
[[Category: Matte A]]
[[Category: Matte, A]]
[[Category: Shi R]]
[[Category: Shi, R]]
[[Category: Bsgi]]
[[Category: Fad binding domain]]
[[Category: Rna binding protein]]
[[Category: Trna modification]]

Latest revision as of 09:34, 21 February 2024

Crystal Structure of E.coli MnmG (GidA), a Highly-Conserved tRNA Modifying Enzyme

3ces, resolution 2.41Å

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