1OZV
Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy
Summary for 1OZV
| Entry DOI | 10.2210/pdb1ozv/pdb |
| Related | 1MLV |
| Descriptor | Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplast, LYSINE, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total) |
| Functional Keywords | set domain, lysine n-methylation, multiple 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 | 153482.30 |
| Authors | Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H. (deposition date: 2003-04-09, release date: 2003-07-01, Last modification date: 2023-08-16) |
| Primary citation | Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H. Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT Nat.Struct.Biol., 10:545-552, 2003 Cited by PubMed Abstract: SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys. PubMed: 12819771DOI: 10.1038/nsb946 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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