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Crystal structure of SAM‐dependent methyltransferase from Pyrococcus horikoshii

Crystal structure of SAM‐dependent methyltransferase from Pyrococcus horikoshii 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystal structure of SAM‐dependent methyltransferase from Pyrococcus horikoshii

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Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17016648
pmid
29199993
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2017

Keywords: ; ; ;

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