5ii8: Difference between revisions

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-'''Unreleased structure'''
-The entry 5ii8 is ON HOLD  until Paper Publication
+==Orthorhombic crystal structure of red abalone lysin at 0.99 A resolution==
+<StructureSection load='5ii8' size='340' side='right'caption='[[5ii8]], [[Resolution|resolution]] 0.99&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ii8]] is a 1 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=5II8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5II8 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]] 0.99&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ii8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii8 OCA], [https://pdbe.org/5ii8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ii8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ii8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii8 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ii8" 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]]