5YPT
Crystal structure of Marchantia paleacea chalone synthase like 1 (CHSL1)
Summary for 5YPT
| Entry DOI | 10.2210/pdb5ypt/pdb |
| Descriptor | Stilbenecarboxylate synthase 1 (2 entities in total) |
| Functional Keywords | chalcone synthase, pks type iii, chsl1, transferase |
| Biological source | Marchantia polymorpha (Liverwort) |
| Total number of polymer chains | 6 |
| Total formula weight | 279575.15 |
| Authors | |
| Primary citation | Yu, H.N.,Liu, X.Y.,Gao, S.,Sun, B.,Zheng, H.B.,Ji, M.,Cheng, A.X.,Lou, H.X. Structural and biochemical characterization of the plant type III polyketide synthases of the liverwort Marchantia paleacea. Plant Physiol. Biochem., 125:95-105, 2018 Cited by PubMed Abstract: Chalcone synthases (CHSs) of the type III polyketide synthases (PKSs), catalyze the formation of a tetraketide intermediate from a CoA-tethered starter and malonyl-CoA but use different cyclization mechanisms to produce distinct chemical scaffolds. Herein, we characterized CHS and CHS-like enzymes (designated MpCHS and MpCHSL1, 2 and 3) from Marchantia paleacea and determined the crystal structure of MpCHSL1. MpCHS catalyzed a Claisen condensation to form chalcone, while MpCHSLs catalyzed the formation of lactonized α-pyrones in vitro. Based on the structural, mutational and in vitro biochemical analyses, we established that MpCHSL1 is structurally and functionally closer to prototype CHS than stilbene synthase, and characterized the structural basis for the functional diversity of the type III PKSs. A chalcone-forming mutant of MpCHSL1 was build directed by the structural information. These findings pave the way for future studies to elucidate the functional diversity of type III PKSs in liverwort. PubMed: 29428820DOI: 10.1016/j.plaphy.2018.01.030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.394 Å) |
Structure validation
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