2lyn: Difference between revisions

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-{{Seed}}
-[[Image:2lyn.png|left|200px]]
-<!--
+==HIGH RESOLUTION STRUCTURE OF RED ABALONE LYSIN DIMER==
-The line below this paragraph, containing "STRUCTURE_2lyn", creates the "Structure Box" on the page.
+<StructureSection load='2lyn' size='340' side='right'caption='[[2lyn]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2lyn]] is a 4 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=2LYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LYN FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07&#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=2lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyn OCA], [https://pdbe.org/2lyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lyn RCSB], [https://www.ebi.ac.uk/pdbsum/2lyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyn ProSAT]</span></td></tr>
-{{STRUCTURE_2lyn|  PDB=2lyn  |  SCENE=  }}
+</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/2lyn_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=2lyn ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===HIGH RESOLUTION STRUCTURE OF RED ABALONE LYSIN DIMER===
+.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<ref>PMID:10666624</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2lyn" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10666624}}, adds the Publication Abstract to the page
+*[[Lysin 3D structures|Lysin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10666624 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10666624}}
+__TOC__
+</StructureSection>
-==About this Structure==
-LYN is a 4 chains structure of sequences 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=2LYN OCA].
-==Reference==
-<ref group="xtra">PMID:10666624</ref><references group="xtra"/>
 [[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: Fertilization protein]]
-[[Category: Gamete recognition protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:07:41 2009''