Crystal structure of SAM-dependent methyltransferase from \it Pyrococcus horikoshii

Pampa, K. J. and Madan Kumar, S. and Hema, M. K. and Kumara, Karthik and Naveen, S. and Kunishima, Naoki and Lokanath, N. K. (2017) Crystal structure of SAM-dependent methyltransferase from \it Pyrococcus horikoshii. Acta Crystallographica Section F, 73 (12). pp. 706-712. ISSN 2053-230X

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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 \it S-adenosyl-\sc l-methionine (SAM) is used for catalysis by SAM-dependent methyltransferases (SAM-MTs). The crystal structure of \it Pyrococcus horikoshii SAM-MT was determined to a resolution of 2.1Å 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.

Item Type: Article
Uncontrolled Keywords: methyltransferases, Rossmann-like fold, SAM-binding residues, Pyrococcus horikoshii
Subjects: B Life Science > Biotechnology
Divisions: Department of > Biotechnology
Depositing User: C Swapna Library Assistant
Date Deposited: 19 Jun 2019 10:21
Last Modified: 19 Jun 2019 10:21

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