3vgz
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of E. coli YncE== | |
| + | <StructureSection load='3vgz' size='340' side='right'caption='[[3vgz]], [[Resolution|resolution]] 1.70Å' 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]] 1.7Å</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®/PubMed®, 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]] | ||
Current revision
Crystal structure of E. coli YncE
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