3KHC
Crystal Structure of Escherichia coli AlkB in complex with ssDNA containing a 1-methylguanine lesion
Summary for 3KHC
Entry DOI | 10.2210/pdb3khc/pdb |
Related | 3KHB |
Descriptor | Alpha-ketoglutarate-dependent dioxygenase alkB, DNA (5'-D(P*TP*AP*(MG1)P*TP*GP*CP*CP*T)-3'), DNA (5'-D(P*GP*CP*AP*T)-3'), ... (6 entities in total) |
Functional Keywords | oxidoreductase, 1-methylguanine, alkb, 2-oxoglutarate, dioxygenase, dna damage, dna repair, iron, metal-binding, oxidoreductase-dna complex, oxidoreductase/dna |
Biological source | Escherichia coli K-12 |
Total number of polymer chains | 4 |
Total formula weight | 52736.13 |
Authors | Hollis, T.,Holland, P.J. (deposition date: 2009-10-30, release date: 2010-01-12, Last modification date: 2023-09-06) |
Primary citation | Holland, P.J.,Hollis, T. Structural and mutational analysis of Escherichia coli AlkB provides insight into substrate specificity and DNA damage searching. Plos One, 5:e8680-e8680, 2010 Cited by PubMed Abstract: In Escherichia coli, cytotoxic DNA methyl lesions on the N1 position of purines and N3 position of pyrimidines are primarily repaired by the 2-oxoglutarate (2-OG) iron(II) dependent dioxygenase, AlkB. AlkB repairs 1-methyladenine (1-meA) and 3-methylcytosine (3-meC) lesions, but it also repairs 1-methylguanine (1-meG) and 3-methylthymine (3-meT) at a much less efficient rate. How the AlkB enzyme is able to locate and identify methylated bases in ssDNA has remained an open question. PubMed: 20084272DOI: 10.1371/journal.pone.0008680 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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