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5mr2

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Crystal structure of red abalone VERL repeat 2 with linker at 2.5 A resolution

Structural highlights

5mr2 is a 3 chain structure with sequence from Haliotis rufescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5mr2"

@@ Line 1: / Line 1: @@
 ==Crystal structure of red abalone VERL repeat 2 with linker at 2.5 A resolution==
-<StructureSection load='5mr2' size='340' side='right' caption='[[5mr2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='5mr2' size='340' side='right'caption='[[5mr2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5mr2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MR2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5mr2]] is a 3 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=5MR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MR2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ii4|5ii4]], [[5ii5|5ii5]], [[5ii6|5ii6]], [[5iia|5iia]], [[5iib|5iib]], [[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk3|3nk3]], [[3nk4|3nk4]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5mr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mr2 OCA], [http://pdbe.org/5mr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mr2 RCSB], [http://www.ebi.ac.uk/pdbsum/5mr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mr2 ProSAT]</span></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=5mr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mr2 OCA], [https://pdbe.org/5mr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mr2 RCSB], [https://www.ebi.ac.uk/pdbsum/5mr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mr2 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Al-Hosseini, H Sadat]]
+[[Category: Haliotis rufescens]]
-[[Category: Jovine, L]]
+[[Category: Large Structures]]
-[[Category: Nishimura, K]]
+[[Category: De Sanctis D]]
-[[Category: Raj, I]]
+[[Category: Jovine L]]
-[[Category: Sanctis, D De]]
+[[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]]

5mr2

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Current revision

Crystal structure of red abalone VERL repeat 2 with linker at 2.5 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

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