4ce7

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Crystal structure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradationCrystal structure of a novel unsaturated beta-glucuronyl hydrolase enzyme, belonging to family GH105, involved in ulvan degradation

Structural highlights

4ce7 is a 3 chain structure with sequence from Nonlabens ulvanivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UH105_NONUL] Glucuronyl hydrolase involved in ulvan degradation. Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl). Unsaturated 3S-rhamnoglycuronyl hydrolase works together with ulvan lyases to fully degrade the ulvan polymer, catalyzing specifically the cleavage of the unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) of deltaUA-Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides, the end products of the ulvan lyase reaction. Also hydrolases deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-GlcA-Rha3S tetrasaccharidestetrasaccharides. Prefers tetrasaccharides over disaccharides and prefers an uronic residue at subsite +2.[1]

References

  1. Nyvall-Collen P, Jeudy A, Sassi JF, Groisillier A, Czjzek M, Coutinho PM, Helbert W. A novel unsaturated beta-glucuronyl hydrolase involved in ulvan degradation unveils the versatility of stereochemistry requirements in family GH105. J Biol Chem. 2014 Jan 9. PMID:24407291 doi:http://dx.doi.org/10.1074/jbc.M113.537480

4ce7, resolution 1.90Å

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