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Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.

ABSTRACT: 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?Å 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.

SUBMITTER: Pampa KJ

PROVIDER: S-EPMC5713677 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.

Pampa K J KJ Madan Kumar S S Hema M K MK Kumara Karthik K Naveen S S Kunishima Naoki N Lokanath N K NK

Acta crystallographica. Section F, Structural biology communications 20171124 Pt 12

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 Å using X-ray diffraction. The monomeric structure consists of a Rossmann-like fold (domain I ...[more]

PMID: 29199993

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