3BVS
Crystal Structure of Bacillus cereus Alkylpurine DNA Glycosylase AlkD
Summary for 3BVS
| Entry DOI | 10.2210/pdb3bvs/pdb |
| Descriptor | Alkylpurine DNA Glycosylase AlkD (2 entities in total) |
| Functional Keywords | dna glycosylase, heat repeat, alkylpurine, dna repair, hydrolase |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 28423.88 |
| Authors | Rubinson, E.H.,Eichman, B.F. (deposition date: 2008-01-07, release date: 2008-07-15, Last modification date: 2024-02-21) |
| Primary citation | Rubinson, E.H.,Metz, A.H.,O'Quin, J.,Eichman, B.F. A New Protein Architecture for Processing Alkylation Damaged DNA: The Crystal Structure of DNA Glycosylase AlkD. J.Mol.Biol., 381:13-23, 2008 Cited by PubMed Abstract: DNA glycosylases safeguard the genome by locating and excising chemically modified bases from DNA. AlkD is a recently discovered bacterial DNA glycosylase that removes positively charged methylpurines from DNA, and was predicted to adopt a protein fold distinct from from those of other DNA repair proteins. The crystal structure of Bacillus cereus AlkD presented here shows that the protein is composed exclusively of helical HEAT-like repeats, which form a solenoid perfectly shaped to accommodate a DNA duplex on the concave surface. Structural analysis of the variant HEAT repeats in AlkD provides a rationale for how this protein scaffolding motif has been modified to bind DNA. We report 7mG excision and DNA binding activities of AlkD mutants, along with a comparison of alkylpurine DNA glycosylase structures. Together, these data provide important insight into the requirements for alkylation repair within DNA and suggest that AlkD utilizes a novel strategy to manipulate DNA in its search for alkylpurine bases. PubMed: 18585735DOI: 10.1016/j.jmb.2008.05.078 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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