9JUB

Cryo-EM structure of human hyaluronidase PH-20

Summary for 9JUB

• Entry DOI: 10.2210/pdb9jub/pdb
• EMDB information: 61826
• Descriptor: Hyaluronidase PH-20, Heavy chain of 79C11Fab, Light chain of 79C11Fab, ... (5 entities in total)
• Functional Keywords: hyaluronidase, endoglycosidase hydrolase, fab complex, hydrolase, hydrolase-immune system complex, hydrolase/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 92633.18

Authors

Im, S.-B.,Jeong, T.-K.,Kim, N.,Oh, B.-H. (deposition date: 2024-10-07, release date: 2024-10-30, Last modification date: 2025-04-16)

Primary citation

Im, S.B.,Song, H.N.,Jeong, T.K.,Kim, N.,Kim, K.,Park, S.J.,Oh, B.H.
Cryo-EM Structure of Human Hyaluronidase PH-20.
Proteins, 93:1067-1073, 2025

PubMed Abstract: PH-20 is a specific type of hyaluronidase that plays a critical role in the fertilization process by facilitating the initial binding of sperm to the glycoprotein layer surrounding the oocyte and subsequently breaking down hyaluronic acid polymers in the cumulus cell layer. PH-20 contains an epidermal growth factor (EGF)-like domain, which may be involved in the recognition of the glycoprotein layer in addition to the catalytic domain. Herein, we report the structure of human PH-20 determined by cryogenic electron microscopy. Comparative analyses of the PH-20 structure with two other available hyaluronidase structures reveal a general similarity in the central catalytic domains, including the conservation of catalytically essential residues at the equivalent spatial positions. However, unique difference is found in the EGF-like domain, characterized by a longer sequence that is likely to form a flexibly anchored β-hairpin containing a disulfide bond.

PubMed: 39722545
DOI: 10.1002/prot.26788

Experimental method

ELECTRON MICROSCOPY (3.1 Å)