2J6A

Structure of S. cerevisiae Trm112 protein, a methyltransferase activator

Summary for 2J6A

• Entry DOI: 10.2210/pdb2j6a/pdb
• Descriptor: PROTEIN TRM112, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• Functional Keywords: translation termination, methyltransferase, transferase, erf1, nuclear protein, protein methylation
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 16034.57

Authors

Heurgue-Hamard, V.,Graille, M.,Scrima, N.,Ulryck, N.,Champ, S.,Van Tilbeurgh, H.,Buckingham, R.H. (deposition date: 2006-09-27, release date: 2006-09-28, Last modification date: 2024-05-08)

Primary citation

Heurgue-Hamard, V.,Graille, M.,Scrima, N.,Ulryck, N.,Champ, S.,Van Tilbeurgh, H.,Buckingham, R.H.
The Zinc Finger Protein Ynr046W is Plurifunctional and a Component of the Erf1 Methyltransferase in Yeast.
J.Biol.Chem., 281:36140-, 2006

PubMed Abstract: Protein release factor eRF1 in Saccharomyces cerevisiae, in complex with eRF3 and GTP, is methylated on a functionally crucial Gln residue by the S-adenosylmethionine-dependent methyltransferase Ydr140w. Here we show that eRF1 methylation, in addition to these previously characterized components, requires a 15-kDa zinc-binding protein, Ynr046w. Co-expression in Escherichia coli of Ynr046w and Ydr140w allows the latter to be recovered in soluble form rather than as inclusion bodies, and the two proteins co-purify on nickel-nitrilotriacetic acid chromatography when Ydr140w alone carries a His tag. The crystal structure of Ynr046w has been determined to 1.7 A resolution. It comprises a zinc-binding domain built from both the N- and C-terminal sequences and an inserted domain, absent from bacterial and archaeal orthologs of the protein, composed of three alpha-helices. The active methyltransferase is the heterodimer Ydr140w.Ynr046w, but when alone, both in solution and in crystals, Ynr046w appears to be a homodimer. The Ynr046w eRF1 methyltransferase subunit is shared by the tRNA methyltransferase Trm11p and probably by two other enzymes containing a Rossman fold.

PubMed: 17008308
DOI: 10.1074/JBC.M608571200

Experimental method

X-RAY DIFFRACTION (1.7 Å)