1ve3

Publication Abstract from PubMed

Methyltransferases (MTs) are enzymes involved in methylation that are needed to perform cellular processes such as biosynthesis, metabolism, gene expression, protein trafficking and signal transduction. The cofactor S-adenosyl-L-methionine (SAM) is used for catalysis by SAM-dependent methyltransferases (SAM-MTs). The crystal structure of Pyrococcus horikoshii SAM-MT was determined to a resolution of 2.1 A using X-ray diffraction. The monomeric structure consists of a Rossmann-like fold (domain I) and a substrate-binding domain (domain II). The cofactor (SAM) molecule binds at the interface between adjacent subunits, presumably near to the active site(s) of the enzyme. The observed dimeric state might be important for the catalytic function of the enzyme.

Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.,Pampa KJ, Madan Kumar S, Hema MK, Kumara K, Naveen S, Kunishima N, Lokanath NK Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):706-712. doi:, 10.1107/S2053230X17016648. Epub 2017 Nov 24. PMID:29199993^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.