3w9z

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Current revision (08:44, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3w9z' size='340' side='right'caption='[[3w9z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3w9z' size='340' side='right'caption='[[3w9z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3w9z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3w9z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vhn|1vhn]], [[3b0p|3b0p]], [[3b0u|3b0u]], [[3b0v|3b0v]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2140, dusC, JW2128, yohI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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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=3w9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9z OCA], [https://pdbe.org/3w9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9z RCSB], [https://www.ebi.ac.uk/pdbsum/3w9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9z 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=3w9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9z OCA], [https://pdbe.org/3w9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9z RCSB], [https://www.ebi.ac.uk/pdbsum/3w9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DUSC_ECOLI DUSC_ECOLI]] Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
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[https://www.uniprot.org/uniprot/DUSC_ECOLI DUSC_ECOLI] Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dihydrouridine (D) is one of the most widely conserved tRNA modifications. Dihydrouridine synthase (Dus) is responsible for introducing D modifications into RNA by the reduction of uridine. Recently, a unique substrate-recognition mechanism using a small adapter molecule has been proposed for Thermus thermophilus Dus (TthDusC). To acquire insight regarding its substrate-recognition mechanism, the crystal structure of DusC from Escherichia coli (EcoDusC) was determined at 2.1 A resolution. EcoDusC was shown to be composed of two domains: an N-terminal catalytic domain and a C-terminal tRNA-binding domain. An L-shaped electron density surrounded by highly conserved residues was found in the active site, as observed for TthDus. Structure comparison with TthDus indicated that the N-terminal region has a similar structure, whereas the C-terminal domain has marked differences in its relative orientation to the N-terminal domain as well as in its own structure. These observations suggested that Dus proteins adopt a common substrate-recognition mechanism using an adapter molecule, whereas the manner of tRNA binding is diverse.
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Structure of dihydrouridine synthase C (DusC) from Escherichia coli.,Chen M, Yu J, Tanaka Y, Tanaka M, Tanaka I, Yao M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):834-8. doi:, 10.1107/S1744309113019489. Epub 2013 Jul 27. PMID:23908023<ref>PMID:23908023</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3w9z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, M]]
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[[Category: Chen M]]
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[[Category: Tanaka, I]]
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[[Category: Tanaka I]]
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[[Category: Tanaka, Y]]
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[[Category: Tanaka Y]]
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[[Category: Yao, M]]
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[[Category: Yao M]]
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[[Category: Yu, J]]
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[[Category: Yu J]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]
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[[Category: Tim barrel]]
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[[Category: Trna]]
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Current revision

Crystal structure of DusC

PDB ID 3w9z

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