5UBB
Crystal structure of human alpha N-terminal protein methyltransferase 1B
Summary for 5UBB
| Entry DOI | 10.2210/pdb5ubb/pdb |
| Descriptor | Alpha N-terminal protein methyltransferase 1B, S-ADENOSYLMETHIONINE, UNKNOWN ATOM OR ION, ... (4 entities in total) |
| Functional Keywords | methyl transferase, structural genomics, structural genomics consortium, sgc, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25404.13 |
| Authors | Dong, C.,Zhu, L.,Tempel, W.,Dong, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2016-12-20, release date: 2017-03-22, Last modification date: 2024-03-06) |
| Primary citation | Dong, C.,Dong, G.,Li, L.,Zhu, L.,Tempel, W.,Liu, Y.,Huang, R.,Min, J. An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2. Commun Biol, 1:183-183, 2018 Cited by PubMed Abstract: α-N-terminal methylation of proteins is an important post-translational modification that is catalyzed by two different N-terminal methyltransferases, namely NTMT1 and NTMT2. Previous studies have suggested that NTMT1 is a tri-methyltransferase, whereas NTMT2 is a mono-methyltransferase. Here, we report the first crystal structures, to our knowledge, of NTMT2 in binary complex with S-adenosyl-L-methionine as well as in ternary complex with S-adenosyl-L-homocysteine and a substrate peptide. Our structural observations combined with biochemical studies reveal that NTMT2 is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide, otherwise it is predominantly a mono-methyltransferase. The residue N89 of NTMT2 serves as a gatekeeper residue that regulates the binding of unmethylated versus monomethylated substrate peptide. Structural comparison of NTMT1 and NTMT2 prompts us to design a N89G mutant of NTMT2 that can profoundly alter its catalytic activities and product specificities. PubMed: 30417120DOI: 10.1038/s42003-018-0196-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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