5OSQ

ZP-N domain of mammalian sperm receptor ZP3 (crystal form II, processed in P21221)

Summary for 5OSQ

• Entry DOI: 10.2210/pdb5osq/pdb
• Related: 3D4C 3D4G 3EF7 3NK3 3NK4
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein,Zona pellucida sperm-binding protein 3, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: fertilization, oocyte, egg coat, zona pellucida, vitelline envelope, zp domain, egg-sperm interaction, species-specific gamete recognition, speciation, biodiversity, infertility, extracellular matrix, immunoglobulin-like fold, glycoprotein, receptor, secreted, transmembrane, cell adhesion
• Biological source: Escherichia coli K-12; More
• Cellular location: Processed zona pellucida sperm-binding protein 3: Secreted, extracellular space, extracellular matrix . Cell membrane ; Single-pass type I membrane protein : P10761
• Total number of polymer chains: 2
• Total formula weight: 106973.12

Authors

Jovine, L.,Monne, M. (deposition date: 2017-08-18, release date: 2017-09-06, Last modification date: 2024-10-23)

Primary citation

Monne, M.,Han, L.,Schwend, T.,Burendahl, S.,Jovine, L.
Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats
Nature, 456:653-, 2008

PubMed Abstract: Species-specific recognition between the egg extracellular matrix (zona pellucida) and sperm is the first, crucial step of mammalian fertilization. Zona pellucida filament components ZP3 and ZP2 act as sperm receptors, and mice lacking either of the corresponding genes produce oocytes without a zona pellucida and are completely infertile. Like their counterparts in the vitelline envelope of non-mammalian eggs and many other secreted eukaryotic proteins, zona pellucida subunits polymerize using a 'zona pellucida (ZP) domain' module, whose conserved amino-terminal part (ZP-N) was suggested to constitute a domain of its own. No atomic structure has been reported for ZP domain proteins, and there is no structural information on any conserved vertebrate protein that is essential for fertilization and directly involved in egg-sperm binding. Here we describe the 2.3 ångström (A) resolution structure of the ZP-N fragment of mouse primary sperm receptor ZP3. The ZP-N fold defines a new immunoglobulin superfamily subtype with a beta-sheet extension characterized by an E' strand and an invariant tyrosine residue implicated in polymerization. The structure strongly supports the presence of ZP-N repeats within the N-terminal region of ZP2 and other vertebrate zona pellucida/vitelline envelope proteins, with implications for overall egg coat architecture, the post-fertilization block to polyspermy and speciation. Moreover, it provides an important framework for understanding human diseases caused by mutations in ZP domain proteins and developing new methods of non-hormonal contraception.

PubMed: 19052627
DOI: 10.1038/NATURE07599

Experimental method

X-RAY DIFFRACTION (2.05 Å)