8QD6
AntI Ser245DHA (PMSF)
Summary for 8QD6
| Entry DOI | 10.2210/pdb8qd6/pdb |
| Related | 6HXA |
| Descriptor | Photorhabdus luminescens subsp. laumondii TTO1 complete genome segment 15/17, SODIUM ION, TETRAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | natural product biosynthesis, polyketide synthase system, alpha, beta-hydrolase fold, polyketide shortening, retro claisen reaction, lyase |
| Biological source | Photorhabdus laumondii subsp. laumondii TTO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 46284.69 |
| Authors | Schmalhofer, M.,Vagstad, A.L.,Zhou, Q.,Bode, H.B.,Groll, M. (deposition date: 2023-08-28, release date: 2024-03-13, Last modification date: 2024-06-19) |
| Primary citation | Schmalhofer, M.,Vagstad, A.L.,Zhou, Q.,Bode, H.B.,Groll, M. Polyketide Trimming Shapes Dihydroxynaphthalene-Melanin and Anthraquinone Pigments. Adv Sci, 11:e2400184-e2400184, 2024 Cited by PubMed Abstract: Pigments such as anthraquinones (AQs) and melanins are antioxidants, protectants, or virulence factors. AQs from the entomopathogenic bacterium Photorhabdus laumondii are produced by a modular type II polyketide synthase system. A key enzyme involved in AQ biosynthesis is PlAntI, which catalyzes the hydrolysis of the bicyclic-intermediate-loaded acyl carrier protein, polyketide trimming, and assembly of the aromatic AQ scaffold. Here, multiple crystal structures of PlAntI in various conformations and with bound substrate surrogates or inhibitors are reported. Structure-based mutagenesis and activity assays provide experimental insights into the three sequential reaction steps to yield the natural product AQ-256. For comparison, a series of ligand-complex structures of two functionally related hydrolases involved in the biosynthesis of 1,8-dihydroxynaphthalene-melanin in pathogenic fungi is determined. These data provide fundamental insights into the mechanism of polyketide trimming that shapes pigments in pro- and eukaryotes. PubMed: 38491909DOI: 10.1002/advs.202400184 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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