5EMH
Crystal structure of Iridoid Synthase from Cantharanthus roseus in complex with NADP+
Summary for 5EMH
| Entry DOI | 10.2210/pdb5emh/pdb |
| Descriptor | Iridoid synthase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | reductase, complex, nadph, oxidoreductase |
| Biological source | Catharanthus roseus (Madagascar periwinkle) |
| Total number of polymer chains | 1 |
| Total formula weight | 42434.21 |
| Authors | Sandholu, A.,Thulasiram, H.V.,Kulkarni, K.A. (deposition date: 2015-11-06, release date: 2015-11-25, Last modification date: 2023-11-08) |
| Primary citation | Sandholu, A.S.,Mohole, M.,Duax, W.L.,Thulasiram, H.V.,Sengupta, D.,Kulkarni, K. Dynamics of loops at the substrate entry channel determine the specificity of iridoid synthases. FEBS Lett., 592:2624-2635, 2018 Cited by PubMed Abstract: Iridoid synthases belong to the family of short-chain dehydrogenase/reductase involved in the biosynthesis of iridoids. Despite having high sequence and structural homology with progesterone 5β-reductase, these enzymes exhibit differential substrate specificities. Previously, two loops, L1 and L2 at substrate-binding pocket, were suggested to be involved in generating substrate specificity. However, the structural basis of specificity determinants was elusive. Here, combining sequence and structural analysis, site-directed mutagenesis, and molecular dynamics simulations, we have shown that iridoid synthase contains two channels for substrate entry whose geometries are altered by L1-L2 dynamics, primarily orchestrated by interactions of residues Glu161 and Gly162 of L1 and Asn358 of L2. A complex interplay of these interactions confer the substrate specificity to the enzyme. PubMed: 29944733DOI: 10.1002/1873-3468.13174 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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