1MLV

Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase

Summary for 1MLV

• Entry DOI: 10.2210/pdb1mlv/pdb
• Descriptor: Ribulose-1,5 biphosphate carboxylase/oxygenase large subunit N-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: set domain, lysine n-methylation, photosynthesis, post-translational modification, transferase
• Biological source: Pisum sativum (pea)
• Cellular location: Plastid, chloroplast: Q43088
• Total number of polymer chains: 3
• Total formula weight: 153755.63

Authors

Trievel, R.C.,Beach, B.M.,Dirk, L.M.A.,Houtz, R.L.,Hurley, J.H. (deposition date: 2002-08-30, release date: 2002-10-30, Last modification date: 2024-02-14)

Primary citation

Trievel, R.C.,Beach, B.M.,Dirk, L.M.,Houtz, R.L.,Hurley, J.H.
Structure and catalytic mechanism of a SET domain protein methyltransferase.
Cell(Cambridge,Mass.), 111:91-103, 2002

PubMed Abstract: Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of Rubisco large subunit methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine and a HEPES ion reveals an all-beta architecture for the SET domain embedded within a larger alpha-helical enzyme fold. Conserved regions of the SET domain bind S-adenosylmethionine and substrate lysine at two sites connected by a pore. We propose that methyl transfer is catalyzed by a conserved Tyr at a narrow pore connecting the sites. The cofactor enters by a "back door" on the opposite side of the enzyme from substrate, promoting highly specific protein recognition and allowing addition of multiple methyl groups.

PubMed: 12372303
DOI: 10.1016/S0092-8674(02)01000-0

Experimental method

X-RAY DIFFRACTION (2.6 Å)