4cis: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cis OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cis RCSB], [http://www.ebi.ac.uk/pdbsum/4cis PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cis OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cis RCSB], [http://www.ebi.ac.uk/pdbsum/4cis PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
Living organisms protect the genome against external influences by recognizing and repairing damaged DNA. A common source of gene mutation is the oxidized guanine, which undergoes base excision repair through cleavage of the glycosidic bond between the ribose and the nucleobase of the lesion. We unravel the repair mechanism utilized by bacterial glycosylase, MutM, using quantum-chemical calculations involving more than 1000 atoms of the catalytic site. In contrast to the base-protonated pathway currently favored in the literature, we show that the initial protonation of the lesion's ribose paves the way for an almost barrier-free glycosidic cleavage. The combination of theoretical and experimental data provides further insight into the selectivity and discrimination of MutM's binding site toward various substrates. | |||
Ribose-Protonated DNA Base Excision Repair: A Combined Theoretical and Experimental Study.,Sadeghian K, Flaig D, Blank ID, Schneider S, Strasser R, Stathis D, Winnacker M, Carell T, Ochsenfeld C Angew Chem Int Ed Engl. 2014 Jul 25. doi: 10.1002/anie.201403334. PMID:25065673<ref>PMID:25065673</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 05:29, 7 August 2014
Structure of MutM in complex with carbocyclic 8-oxo-G containing DNAStructure of MutM in complex with carbocyclic 8-oxo-G containing DNA
Structural highlights
Publication Abstract from PubMedLiving organisms protect the genome against external influences by recognizing and repairing damaged DNA. A common source of gene mutation is the oxidized guanine, which undergoes base excision repair through cleavage of the glycosidic bond between the ribose and the nucleobase of the lesion. We unravel the repair mechanism utilized by bacterial glycosylase, MutM, using quantum-chemical calculations involving more than 1000 atoms of the catalytic site. In contrast to the base-protonated pathway currently favored in the literature, we show that the initial protonation of the lesion's ribose paves the way for an almost barrier-free glycosidic cleavage. The combination of theoretical and experimental data provides further insight into the selectivity and discrimination of MutM's binding site toward various substrates. Ribose-Protonated DNA Base Excision Repair: A Combined Theoretical and Experimental Study.,Sadeghian K, Flaig D, Blank ID, Schneider S, Strasser R, Stathis D, Winnacker M, Carell T, Ochsenfeld C Angew Chem Int Ed Engl. 2014 Jul 25. doi: 10.1002/anie.201403334. PMID:25065673[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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