2D51
Pentaketide chromone synthase (M207G mutant)
Summary for 2D51
| Entry DOI | 10.2210/pdb2d51/pdb |
| Related | 1BQ6 1EE0 2D3M 2D52 |
| Descriptor | pentaketide chromone synthase (2 entities in total) |
| Functional Keywords | pentaketide chromone synthase, chalcone synthase, polyketide synthase, transferase |
| Biological source | Aloe arborescens |
| Total number of polymer chains | 2 |
| Total formula weight | 89583.06 |
| Authors | Kohno, T.,Morita, H. (deposition date: 2005-10-27, release date: 2006-11-14, Last modification date: 2024-10-09) |
| Primary citation | Morita, H.,Kondo, S.,Oguro, S.,Noguchi, H.,Sugio, S.,Abe, I.,Kohno, T. Structural Insight into Chain-Length Control and Product Specificity of Pentaketide Chromone Synthase from Aloe arborescens Chem.Biol., 14:359-369, 2007 Cited by PubMed Abstract: The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides. PubMed: 17462571DOI: 10.1016/j.chembiol.2007.02.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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