5WMM
Crystal structure of an adenylation domain interrupted by a methylation domain (AMA4) from nonribosomal peptide synthetase TioS
Summary for 5WMM
| Entry DOI | 10.2210/pdb5wmm/pdb |
| Descriptor | NRPS, MbtH homologue, (2S)-2-amino-3-methylbutanoyl (2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl hydrogen (S)-phosphate, ... (7 entities in total) |
| Functional Keywords | nonribosomal peptide, thiocoraline, depsipeptide, thiolation, nucleotidyl transferase, n-methylation, biosynthetic protein |
| Biological source | Micromonospora sp. ML1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 112951.57 |
| Authors | Pang, A.H.,Mori, S.,Garneau-Tsodikova, S.,Tsodikov, O.V. (deposition date: 2017-07-30, release date: 2018-03-14, Last modification date: 2023-10-04) |
| Primary citation | Mori, S.,Pang, A.H.,Lundy, T.A.,Garzan, A.,Tsodikov, O.V.,Garneau-Tsodikova, S. Structural basis for backbone N-methylation by an interrupted adenylation domain. Nat. Chem. Biol., 14:428-430, 2018 Cited by PubMed Abstract: 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. PubMed: 29556104DOI: 10.1038/s41589-018-0014-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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