8hcj

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Structure of GH43 family enzyme, Xylan 1, 4 Beta- xylosidase from pseudopedobacter saltansStructure of GH43 family enzyme, Xylan 1, 4 Beta- xylosidase from pseudopedobacter saltans

Structural highlights

8hcj is a 8 chain structure with sequence from Pseudopedobacter saltans DSM 12145. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.566Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F0S5E9_PSESL

Publication Abstract from PubMed

Xylose, a key constituent of the heterogeneous hemicellulose polymer, occurs in lignocellulosic biomass and forms xylan polymers through beta-1,4 glycosidic linkages. The beta-1,4-xylosidase enzyme was isolated from Pseudopedobacter saltans (PsGH43) to find an effective enzyme with enhanced activity to depolymerize xylo-oligosaccharides. beta-1,4-xylosidase belongs to the GH43(1) family as classified in the Carbohydrate-Active Enzyme Database (CAZy). PsGH43(2) was found to be active only on xylose-based substrate, 4NPX(3), with maximum activity occurring at a pH 7 and 30 degrees C (K(m) 1.96 +/- 0.2 mM and V(max) 0.43 mM/min). The study also confirms the influence of Ca(2+) ions on enzymatic activity and thermal stability. Subsequently, native PsGH43 was crystallized at optimum conditions and the structure was determined at 2.5 A resolution. Crystallographic analysis revealed an asymmetric unit containing eight monomers and 16 calcium ions wherein a tetramer constituted the functional unit. Each monomer exhibits a characteristic GH43 N-terminal beta-propeller fold that serves as a catalytic domain accommodating one calcium ion in the centre, while the C-terminal beta-sandwich fold associated with the CBM6(4) family preserves another calcium ion. Our study reveals a novel tetrameric arrangement of beta-1,4-xylosidase which unravels its functional indispensability. This study opens newer avenues to engineer a potential enzyme for biofuel and bioethanol industry.

Deciphering the structural and biochemical aspects of xylosidase from Pseudopedobacter saltans.,Vishwakarma P, Sachdeva E, Thakur A, Ethayathulla AS, Goyal A, Kaur P Int J Biol Macromol. 2024 Dec 19;291:139042. doi: 10.1016/j.ijbiomac.2024.139042. PMID:39708861[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Vishwakarma P, Sachdeva E, Thakur A, Ethayathulla AS, Goyal A, Kaur P. Deciphering the structural and biochemical aspects of xylosidase from Pseudopedobacter saltans. Int J Biol Macromol. 2024 Dec 19;291:139042. PMID:39708861 doi:10.1016/j.ijbiomac.2024.139042

8hcj, resolution 2.57Å

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OCA