6ljl | pdb_00006ljl

Crystal Structure of exoHep-Y390A/H555A complexed with a tetrasaccharide substrate

spinqualitylabelsall models 6ljl, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ljl is a 1 chain structure with sequence from Bacteroides intestinalis DSM 17393. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.73Å Ligands: CA, GCD, IDS, SGN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3C5J6_9BACE Publication Abstract from PubMed Heparinases (Hepases) are critical tools for the studies of highly heterogeneous heparin (HP)/heparan sulfate (HS). However, exolytic heparinases urgently needed for the sequencing of HP/HS chains remain undiscovered. Herein, a type of exolytic heparinases (exoHepases) is identified from the genomes of different bacteria. These exoHepases share almost no homology with known Hepases and prefer to digest HP rather than HS chains by sequentially releasing unsaturated disaccharides from their reducing ends. The structural study of an exoHepase (BIexoHep) shows that an N-terminal conserved DUF4962 superfamily domain is essential to the enzyme activities of these exoHepases, which is involved in the formation of a unique L-shaped catalytic cavity controlling the sequential digestion of substrates through electrostatic interactions. Further, several HP octasaccharides have been preliminarily sequenced by using BIexoHep. Overall, this study fills the research gap of exoHepases and provides urgently needed tools for the structural and functional studies of HP/HS chains. Discovery of exolytic heparinases and their catalytic mechanism and potential application.,Zhang Q, Cao HY, Wei L, Lu D, Du M, Yuan M, Shi D, Chen X, Wang P, Chen XL, Chi L, Zhang YZ, Li F Nat Commun. 2021 Feb 24;12(1):1263. doi: 10.1038/s41467-021-21441-8. PMID:33627653 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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