4ILV: Structure of the Dioxygenase Domain of Sacte_2871, a Novel Dioxygenase Carbohydrate-binding Protein Fusion From the Cellulolytic Bacterium Streptomyces SP. Sirexaa-e

Streptomyces sp. SirexAA-E is a highly cellulolytic bacterium isolated from an insect/microbe symbiotic community. When grown on lignin-containing biomass, it secretes SACTE_2871, an aromatic ring dioxygenase domain fused to a family 5/12 carbohydrate-binding module (CBM 5/12). Here we present structural and catalytic studies of this novel fusion enzyme, thus providing insight into its function. The dioxygenase domain has the core beta-sandwich fold typical of this enzyme family but lacks a dimerization domain observed in other intradiol dioxygenases. Consequently, the x-ray structure shows that the enzyme is monomeric and the Fe(III)-containing active site is exposed to solvent in a shallow depression on a planar surface. Purified SACTE_2871 catalyzes the O2-dependent intradiol cleavage of catechyl compounds from lignin biosynthetic pathways, but not their methylated derivatives. Binding studies show that SACTE_2871 binds synthetic lignin polymers and chitin through the interactions of the CBM 5/12 domain, representing a new binding specificity for this fold-family. Based on its unique structural features and functional properties, we propose that SACTE_2871 contributes to the invasive nature of the insect/microbial community by destroying precursors needed by the plant for de novo lignin biosynthesis as part of its natural wounding response.
PDB ID: 4ILVDownload
MMDB ID: 110129
PDB Deposition Date: 2013/1/1
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.06  Å
Source Organism:
Similar Structures:
Biological Unit for 4ILV: monomeric; determined by author and by software (PISA)
Molecular Components in 4ILV
Label Count Molecule
Protein (1 molecule)
Intradiol Ring-cleavage Dioxygenase
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB