3osp | pdb_00003osp

Structure of rev1

spinqualitylabelsall models 3osp, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3osp is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DCP, MG NonStd Res: 3DR, DOC Gene: O6339, REV1, YOR346W (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Abasic (apurinic/apyrimidinic) sites are among the most abundant DNA lesions in humans, and they present a strong block to replication. They are also highly mutagenic because when replicative DNA polymerases manage to insert a nucleotide opposite the lesion, they prefer to insert an A. Rev1, a member of Y-family DNA polymerases, does not obey the A-rule. This enzyme inserts a C opposite an abasic lesion with much greater catalytic efficiency than an A, G, or T. We present here the structure of yeast Rev1 in ternary complex with DNA containing an abasic lesion and with dCTP as the incoming nucleotide. The structure reveals a mechanism of synthesis across an abasic lesion that differs from that in other polymerases. The lesion is driven to an extrahelical position, and the incorporation of a C is mediated by an arginine (Arg324) that is conserved in all known orthologs of Rev1, including humans. The hydrophobic cavity that normally accommodates the unmodified G is instead filled with water molecules. Since Gs are especially prone to depurination through a spontaneous hydrolysis of the glycosidic bond, the ability of Rev1 to stabilize an abasic lesion in its active site and employ a surrogate arginine to incorporate a C provides a unique means for the "error-free" bypass of this noninstructional lesion. DNA synthesis across an abasic lesion by yeast REV1 DNA polymerase.,Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK J Mol Biol. 2011 Feb 11;406(1):18-28. Epub 2010 Dec 15. PMID:21167175 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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