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[[Image:3lyn.jpg|left|200px]]
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{{STRUCTURE_3lyn|  PDB=3lyn  |  SCENE=  }}
'''STRUCTURE OF GREEN ABALONE LYSIN DIMER'''


==STRUCTURE OF GREEN ABALONE LYSIN DIMER==
<StructureSection load='3lyn' size='340' side='right'caption='[[3lyn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/3lyn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lyn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:10698629</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
3LYN is a [[Single protein]] structure of 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].
</div>
<div class="pdbe-citations 3lyn" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10698629 10698629]
*[[Lysin 3D structures|Lysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haliotis fulgens]]
[[Category: Haliotis fulgens]]
[[Category: Single protein]]
[[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: Fertilization protein]]
[[Category: Gamete recognition protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:06:17 2008''

Latest revision as of 00:32, 28 December 2023

STRUCTURE OF GREEN ABALONE LYSIN DIMER

3lyn, resolution 1.70Å

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