6m9m | pdb_00006m9m

Streptococcus mutans AlkD2 bound to inosine-5'-monophosphate

spinqualitylabelsall models 6m9m, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6m9m is a 1 chain structure with sequence from Streptococcus mutans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.401Å Ligands: CL, IMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KL00_STRMG Publication Abstract from PubMed DNA glycosylases remove aberrant DNA nucleobases as the first enzymatic step of the base excision repair (BER) pathway. The alkyl-DNA glycosylases AlkC and AlkD adopt a unique structure based on alpha-helical HEAT repeats. Both enzymes identify and excise their substrates without a base-flipping mechanism used by other glycosylases and nucleic acid processing proteins to access nucleobases that are otherwise stacked inside the double-helix. Consequently, these glycosylases act on a variety of cationic nucleobase modifications, including bulky adducts, not previously associated with BER. The related non-enzymatic HEAT-like repeat (HLR) proteins, AlkD2, and AlkF, have unique nucleic acid binding properties that expand the functions of this relatively new protein superfamily beyond DNA repair. Here, we review the phylogeny, biochemistry, and structures of the HLR proteins, which have helped broaden our understanding of the mechanisms by which DNA glycosylases locate and excise chemically modified DNA nucleobases. Structural Biology of the HEAT-Like Repeat Family of DNA Glycosylases.,Shi R, Shen XX, Rokas A, Eichman BF Bioessays. 2018 Sep 28. doi: 10.1002/bies.201800133. PMID:30264543 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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