View source for 5mr3


==Crystal structure of red abalone egg VERL repeat 2 with linker in complex with sperm lysin at 1.8 A resolution==
<StructureSection load='5mr3' size='340' side='right'caption='[[5mr3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mr3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MR3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mr3 OCA], [https://pdbe.org/5mr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mr3 RCSB], [https://www.ebi.ac.uk/pdbsum/5mr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mr3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELYS_HALRU ELYS_HALRU] Dissolves the egg vitelline layer nonenzymatically during fertilization. It creates a hole of about 3 mu-m in diameter through which the sperm pass.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.

Structural Basis of Egg Coat-Sperm Recognition at Fertilization.,Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512<ref>PMID:28622512</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mr3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysin 3D structures|Lysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haliotis rufescens]]
[[Category: Large Structures]]
[[Category: De Sanctis D]]
[[Category: Jovine L]]
[[Category: Nishimura K]]
[[Category: Raj I]]
[[Category: Sadat Al-Hosseini H]]