Crystal structure of SAM‐dependent methyltransferase from Pyrococcus horikoshii. Issue 12 (4th December 2017)

• Record Type: Journal Article
• Authors: Pampa, K. J.; Madan Kumar, S.; Hema, M. K.; Kumara, Karthik; Naveen, S.; Kunishima, Naoki; Lokanath, N. K.
• Is Part Of: Acta crystallographica. Volume 73:Issue 12(2017:Dec.)
• Page Start: 706
• Page End: 712
• Publication Date: 2017-12-04
• Subjects: methyltransferases -- Rossmann‐like fold -- SAM‐binding residues -- Pyrococcus horikoshii; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X17016648
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of SAM‐dependent methyltransferase from P. horikoshii in complex with the cofactor SAM was solved by X‐ray diffraction. The monomeric structure consists of a Rossmann‐like fold (domain I) and a substrate‐binding domain (domain II). The cofactor binds at the interface between adjacent subunits. 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.