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

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: 20084272
DOI: 10.1371/journal.pone.0008680

Experimental method

X-RAY DIFFRACTION (2.2 Å)