4NIH

Crystal structure of AlkB E136L mutant protein with cofactors bound to dsDNA containing m6A/A

Summary for 4NIH

• Entry DOI: 10.2210/pdb4nih/pdb
• Related: 4NID 4NIG 4NII
• Descriptor: Alpha-ketoglutarate-dependent dioxygenase AlkB, 5'-D(*TP*AP*GP*GP*TP*AP*AP*(6MA)P*AP*CP*CP*GP*T)-3', 5'-D(*AP*AP*CP*GP*GP*TP*AP*TP*TP*AP*CP*CP*T)-3', ... (7 entities in total)
• Functional Keywords: dna/rna direct repair, jelly-roll fold, dna/rna demethylation repair, fe(ii), 2-kg, oxidoreductase-dna complex, oxidoreductase/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 31131.66

Authors

Yi, C.Q.,Zhu, C.X. (deposition date: 2013-11-06, release date: 2014-04-16, Last modification date: 2024-11-06)

Primary citation

Zhu, C.,Yi, C.
Switching Demethylation Activities between AlkB Family RNA/DNA Demethylases through Exchange of Active-Site Residues.
Angew.Chem.Int.Ed.Engl., 53:3659-3662, 2014

PubMed Abstract: The AlkB family demethylases AlkB, FTO, and ALKBH5 recognize differentially methylated RNA/DNA substrates, which results in their distinct biological roles. Here we identify key active-site residues that contribute to their substrate specificity. Swapping such active-site residues between the demethylases leads to partially switched demethylation activities. Combined evidence from X-ray structures and enzyme kinetics suggests a role of the active-site residues in substrate recognition. Such a divergent active-site sequence may aid the design of selective inhibitors that can discriminate these homologue RNA/DNA demethylases.

PubMed: 24596302
DOI: 10.1002/anie.201310050

Experimental method

X-RAY DIFFRACTION (1.374 Å)