4O1E: Structure Of A Methyltransferase Component In Complex With Mthf Involved In O-demethylation

O-Demethylation by acetogenic or organohalide-respiring bacteria leads to the formation of methyltetrahydrofolate from aromatic methyl ethers. O-Demethylases, which are cobalamin-dependent, three-component enzyme systems, catalyse methyl-group transfers from aromatic methyl ethers to tetrahydrofolate via methylcobalamin intermediates. In this study, crystal structures of the tetrahydrofolate-binding methyltransferase module from a Desulfitobacterium hafniense DCB-2 O-demethylase were determined both in complex with tetrahydrofolate and the product methyltetrahydrofolate. While these structures are similar to previously determined methyltransferase structures, the position of key active-site residues is subtly altered. A strictly conserved Asn is displaced to establish a putative proton-transfer network between the substrate N5 and solvent. It is proposed that this supports the efficient catalysis of methyltetrahydrofolate formation, which is necessary for efficient O-demethylation.
PDB ID: 4O1EDownload
MMDB ID: 126270
PDB Deposition Date: 2013/12/15
Updated in MMDB: 2015/09
Experimental Method:
x-ray diffraction
Resolution: 1.61  Å
Source Organism:
Similar Structures:
Biological Unit for 4O1E: dimeric; determined by author and by software (PISA)
Molecular Components in 4O1E
Label Count Molecule
Proteins (2 molecules)
Dihydropteroate Synthase Dhps
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB