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| | ==HIGH RESOLUTION STRUCTURE OF THE RED ABALONE LYSIN MONOMER== | | ==HIGH RESOLUTION STRUCTURE OF THE RED ABALONE LYSIN MONOMER== |
| - | <StructureSection load='2lis' size='340' side='right' caption='[[2lis]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='2lis' size='340' side='right'caption='[[2lis]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lis]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LIS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lis]] 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=2LIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LIS FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lyn|2lyn]]</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]] 1.35Å</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=2lis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lis OCA], [http://pdbe.org/2lis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lis RCSB], [http://www.ebi.ac.uk/pdbsum/2lis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lis 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=2lis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lis OCA], [https://pdbe.org/2lis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lis RCSB], [https://www.ebi.ac.uk/pdbsum/2lis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lis ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Lysin|Lysin]] | + | *[[Lysin 3D structures|Lysin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Haliotis rufescens]] | | [[Category: Haliotis rufescens]] |
| - | [[Category: Kresge, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Stout, C D]] | + | [[Category: Kresge N]] |
| - | [[Category: Vacquier, V D]] | + | [[Category: Stout CD]] |
| - | [[Category: Abalone lysin]] | + | [[Category: Vacquier VD]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Fertilization protein]]
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| - | [[Category: Gamete recognition protein]]
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| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Abalone sperm use lysin to make a hole in the egg's protective vitelline envelope (VE). When released from sperm, lysin first binds to the VE receptor for lysin (VERL) then dissolves the VE by a non-enzymatic mechanism. The structures of the monomeric and dimeric forms of Haliotis rufescens (red abalone) lysin, previously solved at 1.90 and 2.75 A, respectively, have now been refined to 1.35 and 2.07 A, respectively. The monomeric form of lysin was refined using previously obtained crystallization conditions, while the dimer was solved in a new crystal form with four molecules (two dimers) per asymmetric unit. These high-resolution structures reveal alternate residue conformations, enabling a thorough analysis of the conserved residues contributing to the amphipathic nature of lysin. The availability of five independent high-resolution copies of lysin permits comparisons leading to insights on the local flexibility of lysin and alternative conformations of the hypervariable N-terminus, thought to be involved in species-specific receptor recognition. The new analysis led to the discovery of the basic nature of a cleft formed upon dimerization and a patch of basic residues in the dimer interface. Identification of these features was not possible at lower resolution. In light of this new information, a model explaining the binding of sperm lysin to egg VERL and the subsequent dissolution of the egg VE is proposed.
1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding.,Kresge N, Vacquier VD, Stout CD Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):34-41. PMID:10666624[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kresge N, Vacquier VD, Stout CD. 1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding. Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):34-41. PMID:10666624
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