1ve3
From Proteopedia
Crystal structure of PH0226 protein from Pyrococcus horikoshii OT3
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMethyltransferases (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. References
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