1H8P

Bull seminal plasma PDC-109 fibronectin type II module

Summary for 1H8P

• Entry DOI: 10.2210/pdb1h8p/pdb
• Related: 1PDC
• Descriptor: SEMINAL PLASMA PROTEIN PDC-109, PHOSPHOCHOLINE (3 entities in total)
• Functional Keywords: phosphorylcholine-binding protein
• Biological source: BOS TAURUS (BULL)
• Total number of polymer chains: 2
• Total formula weight: 26359.31

Authors

Wah, D.A.,Fernandez-Tornero, C.,Calvete, J.J.,Romero, A. (deposition date: 2001-02-14, release date: 2002-04-12, Last modification date: 2024-11-06)

Primary citation

Wah, D.A.,Fernandez-Tornero, C.,Sanz, L.,Romero, A.,Calvete, J.J.
Sperm Coating Mechanism from the 1.8 A Crystal Structure of Pdc-109-Phosphorylcholine Complex
Structure, 10:505-, 2002

PubMed Abstract: Bovine seminal plasma PDC-109 binds to sperm surface choline lipids and promotes sperm capacitation by stimulating the efflux of cholesterol and phospholipids. The structure of PDC-109 with bound phosphorylcholine was solved using MAD data of a single platinum site. Its two globular (40 x 50 x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide. The choline binding sites lie at the same face of the molecule. Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction between the quaternary ammonium group and a core tryptophan, plus hydrogen bonding between hydroxyls of exposed tyrosines and the phosphate group. The structure of the PDC-109-oPC complex provides a structural ground for the sperm membrane-coating mechanism underlying PDC-109-induced capacitation.

PubMed: 11937055
DOI: 10.1016/S0969-2126(02)00751-7

Experimental method

X-RAY DIFFRACTION (1.82 Å)