6ail
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE AT 1.3 ANGSTROMS RESOLUTION OF A NOVEL UDG, UdgX, FROM Mycobacterium smegmatis== | |
| + | <StructureSection load='6ail' size='340' side='right'caption='[[6ail]], [[Resolution|resolution]] 1.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ail]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AIL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=6ail FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ail OCA], [http://pdbe.org/6ail PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ail RCSB], [http://www.ebi.ac.uk/pdbsum/6ail PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ail ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Uracil DNA glycosylases (UDGs) are important DNA repair enzymes that excise uracil from DNA, yielding an abasic site. Recently, UdgX, an unconventional UDG with extremely tight binding to DNA containing uracil, was discovered. The structure of UdgX from Mycobacterium smegmatis in complex with DNA shows an overall similarity to that of family 4 UDGs except for a protruding loop at the entrance of the uracil-binding pocket. Surprisingly, H109 in the loop was found to make a covalent bond to the abasic site to form a stable intermediate, while the excised uracil remained in the pocket of the active site. H109 functions as a nucleophile to attack the oxocarbenium ion, substituting for the catalytic water molecule found in other UDGs. To our knowledge, this change from a catalytic water attack to a direct nucleophilic attack by the histidine residue is unprecedented. UdgX utilizes a unique mechanism of protecting cytotoxic abasic sites from exposure to the cellular environment. | ||
| - | + | Covalent binding of uracil DNA glycosylase UdgX to abasic DNA upon uracil excision.,Ahn WC, Aroli S, Kim JH, Moon JH, Lee GS, Lee MH, Sang PB, Oh BH, Varshney U, Woo EJ Nat Chem Biol. 2019 Jun;15(6):607-614. doi: 10.1038/s41589-019-0289-3. Epub 2019 , May 17. PMID:31101917<ref>PMID:31101917</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6ail" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ahn, W C]] | ||
[[Category: Aroli, S]] | [[Category: Aroli, S]] | ||
| - | [[Category: Ahn, W.C]] | ||
[[Category: Varshney, V]] | [[Category: Varshney, V]] | ||
| + | [[Category: Woo, E J]] | ||
| + | [[Category: Base excision]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna repair]] | ||
| + | [[Category: Dna-protein crosslink]] | ||
Revision as of 06:03, 29 May 2019
CRYSTAL STRUCTURE AT 1.3 ANGSTROMS RESOLUTION OF A NOVEL UDG, UdgX, FROM Mycobacterium smegmatis
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