1FIZ

THREE DIMENSIONAL STRUCTURE OF BETA-ACROSIN FROM BOAR SPERMATOZOA

Summary for 1FIZ

• Entry DOI: 10.2210/pdb1fiz/pdb
• Related: 1FIW
• Descriptor: BETA-ACROSIN HEAVY CHAIN, BETA-ACROSIN LIGHT CHAIN, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: anti-parallel beta-barrel, hydrolase
• Biological source: Sus scrofa (pig); More
• Total number of polymer chains: 2
• Total formula weight: 33098.94

Authors

Tranter, R.,Read, J.A.,Jones, R.,Brady, R.L. (deposition date: 2000-08-07, release date: 2000-11-08, Last modification date: 2024-10-30)

Primary citation

Tranter, R.,Read, J.A.,Jones, R.,Brady, R.L.
Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin.
Structure Fold.Des., 8:1179-1188, 2000

PubMed Abstract: Proacrosin is a serine protease found specifically within the acrosomal vesicle of all mammalian spermatozoa. During fertilization proacrosin autoactivates to form beta-acrosin, in which there is a "light" chain cross-linked to a "heavy" chain by two disulphide bonds. beta-acrosin is thought to be multifunctional with roles in acrosomal exocytosis, as a receptor for zona pellucida proteins, and as a protease to facilitate penetration of spermatozoa into the egg.

PubMed: 11080640
DOI: 10.1016/S0969-2126(00)00523-2

Experimental method

X-RAY DIFFRACTION (2.9 Å)