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| | ==Crystal structure of red abalone VERL repeat 3 at 2.9 A resolution== | | ==Crystal structure of red abalone VERL repeat 3 at 2.9 A resolution== |
| - | <StructureSection load='5iic' size='340' side='right' caption='[[5iic]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='5iic' size='340' side='right'caption='[[5iic]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iic]] is a 2 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=5IIC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IIC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iic]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] 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=5IIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IIC 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ii5|5ii5]], [[5ii4|5ii4]], [[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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5iic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iic OCA], [https://pdbe.org/5iic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iic RCSB], [https://www.ebi.ac.uk/pdbsum/5iic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iic 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=5iic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iic OCA], [http://pdbe.org/5iic PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iic RCSB], [http://www.ebi.ac.uk/pdbsum/5iic PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iic ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[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> |
| | <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 K-12]] |
| - | [[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]]
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| - | [[Category: Vitelline envelope]]
| + | |
| Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.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]
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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