This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3w9z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:44, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<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 ==
-
<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>
+
<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>
-
</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>
+
</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>
-
<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>
+
<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>
-
<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>
+
<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 ==
-
[[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.
+
[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.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3w9z" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ecoli]]
+
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chen, M]]
+
[[Category: Chen M]]
-
[[Category: Tanaka, I]]
+
[[Category: Tanaka I]]
-
[[Category: Tanaka, Y]]
+
[[Category: Tanaka Y]]
-
[[Category: Yao, M]]
+
[[Category: Yao M]]
-
[[Category: Yu, J]]
+
[[Category: Yu J]]
-
[[Category: Oxidoreductase]]
+
-
[[Category: Reductase]]
+
-
[[Category: Tim barrel]]
+
-
[[Category: Trna]]
+

Current revision

Crystal structure of DusC

PDB ID 3w9z

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools