6j66

Chondroitin sulfate/dermatan sulfate endolytic 4-O-sulfatase

spinqualitylabelsall models 6j66, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j66 is a 2 chain structure with sequence from Vibrio sp. FC509. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.953Å Ligands: CA, DDZ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0C5AQI9_9VIBR Publication Abstract from PubMed Chondroitin sulfate/dermatan sulfate (CS/DS) sulfatases are potential tools for structural and functional studies of CD/DS chains. In our previous study, a CS/DS 4-O-endosulfatase (endoVB4SF) was identified from a marine bacterium (Wang et al., 2015). Herein, another CS/DS 4-O-sulfatase (exoPB4SF) was identified from a Photobacterium sp. ExoPB4SF shares an 83% identity with endoVB4SF but showed strict exolytic activity. Comparative studies were performed for both enzymes on the basis of biochemical features, substrate-degrading patterns and three-dimensional structures. exoPB4SF exhibited a wider temperature and pH adaptability and better thermostability than endoVB4SF. Furthermore, exoPB4SF is a strict exolytic sulfatase that only releases the sulfate group from the GalNAc residue located at the reducing end, whereas endoVB4SF preferentially removed sulfate esters from the reducing end toward the non-reducing end though its directional degradation property was not strict. In addition, the structure of endoVB4SF was determined by X-ray crystallography at 1.95 A. It adopts a globular conformation with two monomers per asymmetric unit. The exoPB4SF structure was constructed by homology modeling. Molecular docking results showed that although the residues around the catalytic center are conserved, the residues at the active site of endoVB4SF adopted a more favorable conformation for the binding of long CS/DS chains than those of exoPB4SF, which may explain why the two highly homogenous sulfatases possessed different action patterns. The results of this study provide insight into the structure-function relationship of CS/DS endo- and exosulfatases for the first time. Comparative Study of Two Chondroitin Sulfate/Dermatan Sulfate 4-O-Sulfatases With High Identity.,Wang S, Su T, Zhang Q, Guan J, He J, Gu L, Li F Front Microbiol. 2019 Jun 12;10:1309. doi: 10.3389/fmicb.2019.01309. eCollection , 2019. PMID:31244815 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfatase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA