Structural highlights
Function
Q333U7_9ACTN
Publication Abstract from PubMed
Interrupted adenylation domains are enigmatic fusions, in which one enzyme is inserted into another to form a highly unusual bifunctional enzyme. We present the first crystal structure of an interrupted adenylation domain that reveals a unique embedded methyltransferase. The structure and functional data provide insight into how these enzymes N-methylate amino acid precursors en route to nonribosomal peptides.
Structural basis for backbone N-methylation by an interrupted adenylation domain.,Mori S, Pang AH, Lundy TA, Garzan A, Tsodikov OV, Garneau-Tsodikova S Nat Chem Biol. 2018 Mar 19. pii: 10.1038/s41589-018-0014-7. doi:, 10.1038/s41589-018-0014-7. PMID:29556104[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mori S, Pang AH, Lundy TA, Garzan A, Tsodikov OV, Garneau-Tsodikova S. Structural basis for backbone N-methylation by an interrupted adenylation domain. Nat Chem Biol. 2018 Mar 19. pii: 10.1038/s41589-018-0014-7. doi:, 10.1038/s41589-018-0014-7. PMID:29556104 doi:http://dx.doi.org/10.1038/s41589-018-0014-7
