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| | <StructureSection load='3lyn' size='340' side='right'caption='[[3lyn]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3lyn' size='340' side='right'caption='[[3lyn]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lyn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haliotis_fulgens Haliotis fulgens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LYN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliotis_fulgens Haliotis fulgens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LYN FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lyn OCA], [http://pdbe.org/3lyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lyn RCSB], [http://www.ebi.ac.uk/pdbsum/3lyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lyn ProSAT]</span></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]] 1.7Å</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=3lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lyn OCA], [https://pdbe.org/3lyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lyn RCSB], [https://www.ebi.ac.uk/pdbsum/3lyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lyn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ELYS_HALFU ELYS_HALFU]] 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_HALFU ELYS_HALFU] 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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| | [[Category: Haliotis fulgens]] | | [[Category: Haliotis fulgens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kresge, N]] | + | [[Category: Kresge N]] |
| - | [[Category: Stout, C D]] | + | [[Category: Stout CD]] |
| - | [[Category: Vacquier, V D]] | + | [[Category: Vacquier VD]] |
| - | [[Category: Abalone lysin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Fertilization protein]]
| + | |
| - | [[Category: Gamete recognition protein]]
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| Structural highlights
Function
ELYS_HALFU 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 lysin is a 16 kDa acrosomal protein used by sperm to create a hole in the egg vitelline envelope. Lysins from seven California abalone exhibit species-specificity in binding to their egg receptor, and range in sequence identity from 63 % to 90 %. The crystal structure of the sperm lysin dimer from Haliotis fulgens (green abalone) has been determined to 1.71 A by multiple isomorphous replacement. Comparisons with the structure of the lysin dimer from Haliotis rufescens (red abalone) reveal a similar overall fold and conservation of features contributing to lysin's amphipathic character. The two structures do, however, exhibit differences in surface residues and electrostatics. A large clustering of non-conserved surface residues around the waist and clefts of the dimer, and differences in charged residues around these regions, indicate areas of the molecule which may be involved in species-specific egg recognition.
The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor.,Kresge N, Vacquier VD, Stout CD J Mol Biol. 2000 Mar 10;296(5):1225-34. PMID:10698629[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kresge N, Vacquier VD, Stout CD. The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor. J Mol Biol. 2000 Mar 10;296(5):1225-34. PMID:10698629 doi:10.1006/jmbi.2000.3533
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