5uuf

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m (Protected "5uuf" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5uuf is ON HOLD until Paper Publication
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==Bacillus cereus DNA glycosylase AlkD bound to a yatakemycin-adenine nucleobase adduct and DNA containing an abasic site (12-mer product complex)==
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<StructureSection load='5uuf' size='340' side='right' caption='[[5uuf]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5uuf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UUF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=YTA:yatakemycin-adenine+nucleobase+adduct'>YTA</scene>, <scene name='pdbligand=ORP:2-DEOXY-5-PHOSPHONO-RIBOSE'>ORP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uug|5uug]], [[5uuh|5uuh]], [[5uuj|5uuj]]</td></tr>
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<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=5uuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uuf OCA], [http://pdbe.org/5uuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uuf RCSB], [http://www.ebi.ac.uk/pdbsum/5uuf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uuf ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Yatakemycin (YTM) is an extraordinarily toxic DNA alkylating agent with potent antimicrobial and antitumor properties and is the most recent addition to the CC-1065 and duocarmycin family of natural products. Though bulky DNA lesions the size of those produced by YTM are normally removed from the genome by the nucleotide-excision repair (NER) pathway, YTM adducts are also a substrate for the bacterial DNA glycosylases AlkD and YtkR2, unexpectedly implicating base-excision repair (BER) in their elimination. The reason for the extreme toxicity of these lesions and the molecular basis for the way they are eliminated by BER have been unclear. Here, we describe the structural and biochemical properties of YTM adducts that are responsible for their toxicity, and define the mechanism by which they are excised by AlkD. These findings delineate an alternative strategy for repair of bulky DNA damage and establish the cellular utility of this pathway relative to that of NER.
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Authors:
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Toxicity and repair of DNA adducts produced by the natural product yatakemycin.,Mullins EA, Shi R, Eichman BF Nat Chem Biol. 2017 Jul 24. doi: 10.1038/nchembio.2439. PMID:28759018<ref>PMID:28759018</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5uuf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Eichman, B F]]
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[[Category: Mullins, E A]]
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[[Category: Alkylpurine]]
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[[Category: Bulky lesion]]
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[[Category: Dna glycosylase]]
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[[Category: Hydrolase-dna-antibiotic complex]]
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[[Category: Protein-dna complex]]

Revision as of 06:05, 17 August 2017

Bacillus cereus DNA glycosylase AlkD bound to a yatakemycin-adenine nucleobase adduct and DNA containing an abasic site (12-mer product complex)

5uuf, resolution 1.61Å

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