ISDA: 23LO

Deposition Date 2026-02-10

Release Date 2026-05-27

Last Version Date 2026-05-27

Entry Detail

PDB ID:

23LO

Keywords:

BIOSYNTHETIC PROTEIN

Title:

crystal structure of a flavin dependent Baeyer Villiger monooxygenase from Micromonospora lupini NBC_00409 in complex with FAD

Biological Source:

Source Organism(s):

Micromonospora lupini (Taxon ID: 285679)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

3.20 Å

R-Value Free:

0.28

R-Value Work:

0.25

R-Value Observed:

0.26

Space Group:

P 1

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Macromolecular Entities

Protein Blast

Polymer Type:polypeptide(L)
Molecule:flavin dependent Baeyer Villi
Chain IDs:A, B (auth: D), C (auth: G), D (auth: J), E (auth: M), F (auth: P)
Chain Length:511
Number of Molecules:6
Biological Source:Micromonospora lupini

Ligand Molecules

FAD

Primary Citation

Deciphering Early Oxidative Steps in Spirotetronate Biosynthesis Reveals a Two-Enzyme Cascade for Macrocyclic Lactone Formation.

Chen, S, Lin, Z, Zhang, Q, Tan, B, Zhang, X, Zhang, W, Zhang, H, Zhu, Y, Zhang, L, Zhang, C.Show

Org.Lett. ? ? ? (2026)

PMID: 42125861 DOI: 10.1021/acs.orglett.6c01499

Abstact

We decipher functions of three monooxygenases (PasO1, PasO3, and PasO4) in early biosynthetic steps in spirotetronate PA-46101 and demonstrate a PasO4/PasO3 cascade for forging the signature macrocyclic lactone. The P450 PasO4 oxidizes a methyl group to a carboxylate, enabling a regiospecific Baeyer-Villiger oxidation by PasO3. Structural analysis of a PasO3 homologue identifies a carboxylate-binding pocket essential for this strict substrate specificity. This two-enzyme cascade can serve as a portable biocatalytic tool for diversifying spirotetronates.

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Protein

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Primary Citation of related structures

Abstact

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