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5ii4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution== | |
| + | <StructureSection load='5ii4' size='340' side='right'caption='[[5ii4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ii4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5II4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5II4 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]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=5ii4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii4 OCA], [https://pdbe.org/5ii4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ii4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ii4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VERL_HALRU VERL_HALRU] Structural component of the egg vitelline envelope; forms long filaments. Functions as species-specific receptor for the sperm protein lysin; prevents fertilization by sperm from other species. Each VERL chain can bind multiple copies of the sperm protein lysin; this creates a 3 um hole in the egg vitelline envelope through which the sperm passes.<ref>PMID:28622512</ref> <ref>PMID:9192632</ref> [https://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity). | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ii4" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Nishimura | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli O157:H7]] | ||
| + | [[Category: Haliotis rufescens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jovine L]] | ||
| + | [[Category: Nishimura K]] | ||
| + | [[Category: Raj I]] | ||
| + | [[Category: Sadat Al-Hosseini H]] | ||
Current revision
Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution
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