3w9z: Difference between revisions
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==Crystal structure of DusC== | |||
=== | <StructureSection load='3w9z' size='340' side='right' caption='[[3w9z]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3w9z]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W9Z FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vhn|1vhn]], [[3b0p|3b0p]], [[3b0u|3b0u]], [[3b0v|3b0v]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2140, dusC, JW2128, yohI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w9z RCSB], [http://www.ebi.ac.uk/pdbsum/3w9z PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[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: Oxidoreductase]] | ||
[[Category: Reductase]] | [[Category: Reductase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
[[Category: Trna]] | [[Category: Trna]] | ||
