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| | ==Crystal structure of E. coli YncE== | | ==Crystal structure of E. coli YncE== |
| - | <StructureSection load='3vgz' size='340' side='right' caption='[[3vgz]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3vgz' size='340' side='right'caption='[[3vgz]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vgz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VGZ FirstGlance]. <br> | + | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vh0|3vh0]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yncE ([http://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=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> |
| - | <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=3vgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgz OCA], [http://pdbe.org/3vgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vgz RCSB], [http://www.ebi.ac.uk/pdbsum/3vgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vgz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/YNCE_ECOLI YNCE_ECOLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Kagawa, W]] | + | [[Category: Large Structures]] |
| - | [[Category: Kurumizaka, H]] | + | [[Category: Kagawa W]] |
| - | [[Category: Niki, H]] | + | [[Category: Kurumizaka H]] |
| - | [[Category: Sagawa, T]] | + | [[Category: Niki H]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Sagawa T]] |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
YNCE_ECOLI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kagawa W, Sagawa T, Niki H, Kurumizaka H. Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE. Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1045-53. Epub 2011, Nov 5. PMID:22120742 doi:10.1107/S0907444911045033
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