Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7EYO

Crystal structure of leech hyaluronidase

Summary for 7EYO
Entry DOI10.2210/pdb7eyo/pdb
DescriptorHyaluronoglucuronidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total)
Functional Keywordshyaluronidae, gh79, hydrolase
Biological sourceHirudo nipponia (Korean blood-sucking leech)
Total number of polymer chains1
Total formula weight57155.11
Authors
Huang, H.,Hou, X.D.,Rao, Y.J.,Kang, Z. (deposition date: 2021-05-31, release date: 2022-05-25, Last modification date: 2024-10-16)
Primary citationHuang, H.,Hou, X.,Xu, R.,Deng, Z.,Wang, Y.,Du, G.,Rao, Y.,Chen, J.,Kang, Z.
Structure and cleavage pattern of a hyaluronate 3-glycanohydrolase in the glycoside hydrolase 79 family.
Carbohydr Polym, 277:118838-118838, 2022
Cited by
PubMed Abstract: Hyaluronidases have attracted a great deal of interest in the field of medicine due to their fundamental roles in the breakdown of hyaluronan. However, little is known about the catalytic mechanism of the hyaluronate 3-glycanohydrolases. Here, we report the crystal structure and cleavage pattern of a leech hyaluronidase (LHyal), which hydrolyzes the β-1,3-glycosidic bonds of hyaluronan. LHyal exhibits the typical structural features of glycoside hydrolase 79 family but contains a variable 'exo-pocket' loop where basic residues R102 and K103 are the structural determinants of hyaluronan binding. Through analysis of the hydrolysis of even- and odd-numbered hyaluronan oligosaccharides, we demonstrate that hexasaccharide is the shortest natural substrate, which can be cleaved from both the reducing and non-reducing ends to release disaccharides, and pentasaccharides are the smallest fragments for recognition and hydrolysis. These observations provide new insights into the degradation of hyaluronan and the evolutionary relationships of the GH79 family enzymes.
PubMed: 34893255
DOI: 10.1016/j.carbpol.2021.118838
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon