1VE3

Crystal structure of PH0226 protein from Pyrococcus horikoshii OT3

Summary for 1VE3

• Entry DOI: 10.2210/pdb1ve3/pdb
• Descriptor: hypothetical protein PH0226, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: dimer, riken structural genomics/proteomics initiative, rsgi, structural genomics, unknown function, nppsfa, national project on protein structural and functional analyses
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 2
• Total formula weight: 54921.58

Authors

Lokanath, N.K.,Yamamoto, H.,Kunishima, N.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-03-26, release date: 2005-05-24, Last modification date: 2024-10-30)

Primary citation

Pampa, K.J.,Madan Kumar, S.,Hema, M.K.,Kumara, K.,Naveen, S.,Kunishima, N.,Lokanath, N.K.
Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.
Acta Crystallogr.,Sect.F, 73:706-712, 2017

PubMed 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.

PubMed: 29199993
DOI: 10.1107/S2053230X17016648

Experimental method

X-RAY DIFFRACTION (2.1 Å)