1lyn: Difference between revisions

New page: left|200px<br /><applet load="1lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyn, resolution 2.75Å" /> '''CRYSTAL STRUCTURE AN...
 
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'''CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES'''<br />


==Overview==
==CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES==
Lysin is a 16-kD acrosomal protein used by abalone spermatozoa to create a, hole in the egg vitelline envelope (VE) by a nonenzymatic mechanism. The, crystal structure of the lysin monomer is known at 1.9 A resolution. The, surface of the molecule reveals two tracks of basic residues running the, length of one surface of the molecule and a patch of solvent-exposed, hydrophobic residues on the opposite surface. Here we report that lysin, dimerizes via interaction of the hydrophobic patches of monomers. Triton, X-100 dissociates the dimer. The crystal structure of the dimer is, described at 2.75 A resolution. Fluorescence energy transfer experiments, show that the dimer has an approximate KD of 1 microM and that monomers, exchange rapidly between dimers. Addition of isolated egg VE dissociates, dimers, implicating monomers as the active species in the dissolution, reaction. This work represents the first step in the elucidation of the, mechanism by which lysin enables abalone spermatozoa to create a hole in, the egg envelope during fertilization.
<StructureSection load='1lyn' size='340' side='right'caption='[[1lyn]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lyn]] is a 2 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=1LYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LYN 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]] 2.75&#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=1lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyn OCA], [https://pdbe.org/1lyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lyn RCSB], [https://www.ebi.ac.uk/pdbsum/1lyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyn ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
[[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/1lyn_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=1lyn ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LYN OCA].
*[[Lysin 3D structures|Lysin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species., Shaw A, Fortes PA, Stout CD, Vacquier VD, J Cell Biol. 1995 Sep;130(5):1117-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7657696 7657696]
[[Category: Haliotis rufescens]]
[[Category: Haliotis rufescens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Shaw, A.]]
[[Category: Shaw A]]
[[Category: Stout, C.D.]]
[[Category: Stout CD]]
[[Category: Vacquier, V.D.]]
[[Category: Vacquier VD]]
[[Category: fertilization protein]]
 
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