1ve3 | pdb_00001ve3

Crystal structure of PH0226 protein from Pyrococcus horikoshii OT3

spinqualitylabelsall models 1ve3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ve3 is a 2 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MSE, SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function O57965_PYRHO Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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