6AKD
Crystal structure of IdnL7
Summary for 6AKD
| Entry DOI | 10.2210/pdb6akd/pdb |
| Descriptor | AMP-dependent synthetase and ligase, '5'-O-(N-(L-ALANYL)-SULFAMOYL)ADENOSINE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ligase, atp-binding, five layered alpha-beta-alpha-beta-alpha sandwich fold |
| Biological source | Streptomyces sp. ML694-90F3 |
| Total number of polymer chains | 1 |
| Total formula weight | 58116.34 |
| Authors | Cieslak, J.,Miyanaga, A.,Kudo, F.,Eguchi, T. (deposition date: 2018-08-31, release date: 2019-03-06, Last modification date: 2023-11-22) |
| Primary citation | Cieslak, J.,Miyanaga, A.,Takaishi, M.,Kudo, F.,Eguchi, T. Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis. Acta Crystallogr F Struct Biol Commun, 75:299-306, 2019 Cited by PubMed Abstract: Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5'-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids. PubMed: 30950831DOI: 10.1107/S2053230X19002863 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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