7BIO

Crystal structure of monooxygenase RslO4 from Streptomyces bottropensis

Summary for 7BIO

• Entry DOI: 10.2210/pdb7bio/pdb
• Descriptor: Monooxygenase/putative anthronoxygenase, ETHANOL, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: rishirilides biosynthesis, oxidoreductase
• Biological source: Streptomyces bottropensis
• Total number of polymer chains: 2
• Total formula weight: 26771.90

Authors

Zhang, L.,Zuo, C.,Alali, A.,Bechthold, A.,Einsle, O. (deposition date: 2021-01-12, release date: 2021-01-20, Last modification date: 2024-01-31)

Primary citation

Alali, A.,Zhang, L.,Li, J.,Zuo, C.,Wassouf, D.,Yan, X.,Schwarzer, P.,Gunther, S.,Einsle, O.,Bechthold, A.
Biosynthesis of the Tricyclic Aromatic Type II Polyketide Rishirilide: New Potential Third Ring Oxygenation after Three Cyclization Steps.
Mol Biotechnol., 63:502-514, 2021

PubMed Abstract: Rishirilides are a group of PKS II secondary metabolites produced by Streptomyces bottropensis Gö C4/4. Biosynthetic studies in the past have elucidated early and late steps of rishirilide biosynthesis. This work is aiming to solve the remaining steps in the rishirilide biosynthesis. Inactivation of the cyclase gene rslC3 in Streptomyces bottropensis resulted in an interruption of rishirilide production. Instead, accumulation of the tricyclic aromatic galvaquinones was observed. Similar results were observed after deletion of rslO4. Closer inspection into RslO4 crystal structure in addition to site-directed mutagenesis and molecular dynamic simulations revealed that RslO4 might be responsible for quinone formation on the third ring. The RslO1 three-dimensional structure shows a high similarity to FMN-dependent luciferase-like monooxygenases such as the epoxy-forming MsnO8 which acts with the flavin reductase MsnO3 in mensacarcin biosynthesis in the same strain. The high sequence similarity between RslO2 and MsnO3 suggests that RslO2 provides RslO1 with reduced FMN to form an epoxide that serves as substrate for RslO5.

PubMed: 33763824
DOI: 10.1007/s12033-021-00314-x

Experimental method

X-RAY DIFFRACTION (1.795 Å)