3KHB

Crystal structure of Escherichia coli AlkB with Co(II) and 2-OG

Summary for 3KHB

• Entry DOI: 10.2210/pdb3khb/pdb
• Related: 3KHC
• Descriptor: Alpha-ketoglutarate-dependent dioxygenase alkB, COBALT (II) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total)
• Functional Keywords: oxidoreductase, alkb, 2-oxoglutarate, dna alkylation repair, dioxygenase, dna damage, dna repair, iron, metal-binding
• Biological source: Escherichia coli K-12
• Total number of polymer chains: 2
• Total formula weight: 49201.69

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 (2.9 Å)