View source for 3vgz


==Crystal structure of E. coli YncE==
<StructureSection load='3vgz' size='340' side='right'caption='[[3vgz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vgz]] is a 4 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=3VGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VGZ FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3vgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgz OCA], [https://pdbe.org/3vgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vgz RCSB], [https://www.ebi.ac.uk/pdbsum/3vgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vgz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YNCE_ECOLI YNCE_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Propellers are widely utilized in nature as recognition modules. The well conserved beta-propeller fold exhibits a high degree of functional diversity, which is probably accomplished through variations in the surface properties of the proteins. Little is known about the interactions between beta-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial beta-propeller protein YncE binds to DNA. Crystal structures of YncE in the free form and complexed with DNA revealed that the surface region of YncE corresponding to the `canonical' substrate-binding site forms essential contacts with DNA. A single DNA base within a single-stranded DNA region is trapped in the hydrophobic pocket located within the central channel of the beta-propeller protein. These data provide physical evidence for the DNA-binding ability of the previously uncharacterized YncE and also suggest that the `canonical' substrate-binding site may be commonly adapted to facilitate nucleic acid binding in a subset of beta-propeller proteins.

Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE.,Kagawa W, Sagawa T, Niki H, Kurumizaka H Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1045-53. Epub 2011, Nov 5. PMID:22120742<ref>PMID:22120742</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Kagawa W]]
[[Category: Kurumizaka H]]
[[Category: Niki H]]
[[Category: Sagawa T]]