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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of human MTHFR at 2.5 A resolution reveals a unique architecture, appending the well-conserved catalytic TIM-barrel to a eukaryote-only SAM-binding domain. The latter domain provides the predominant interface for MTHFR homo-dimerization and positions the N-terminal serine-rich phosphorylation region near the C-terminal SAM-binding domain. MTHFR phosphorylation, identified on 11 N-terminal residues (16 in total), increases sensitivity to SAM binding and inhibition. The 25-amino-acid inter-domain linker enables conformational plasticity and may be a key mediator of SAM regulation