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| | ==Crystal structure of red abalone VERL repeat 1 with linker at 2.0 A resolution== | | ==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=''> | + | <StructureSection load='5ii4' size='340' side='right'caption='[[5ii4]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ii4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/California_red_abalone California red abalone]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5II4 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ii5|5ii5]], [[5iic|5iic]], [[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk3|3nk3]], [[3nk4|3nk4]], [[5ii6|5ii6]], [[5iia|5iia]], [[5iib|5iib]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VERL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6454 California red abalone]), malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6454 California red abalone])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ii4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii4 OCA], [http://pdbe.org/5ii4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ii4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ii4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: California red abalone]] | + | [[Category: Escherichia coli O157:H7]] |
| - | [[Category: Al-Hosseini, H Sadat]] | + | [[Category: Haliotis rufescens]] |
| - | [[Category: Jovine, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Nishimura, K]] | + | [[Category: Jovine L]] |
| - | [[Category: Raj, I]] | + | [[Category: Nishimura K]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Raj I]] |
| - | [[Category: Egg-sperm interaction]] | + | [[Category: Sadat Al-Hosseini H]] |
| - | [[Category: Fertilization]]
| + | |
| - | [[Category: Gamete recognition]]
| + | |
| - | [[Category: Sperm receptor]]
| + | |
| - | [[Category: Vitelline envelope]]
| + | |
| Structural highlights
Function
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.[1] [2] 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).
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L. Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512 doi:http://dx.doi.org/10.1016/j.cell.2017.05.033
- ↑ Swanson WJ, Vacquier VD. The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule. Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6724-9. PMID:9192632 doi:10.1073/pnas.94.13.6724
- ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L. Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512 doi:http://dx.doi.org/10.1016/j.cell.2017.05.033
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