3lyn: Difference between revisions

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{{Seed}}
[[Image:3lyn.png|left|200px]]


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==STRUCTURE OF GREEN ABALONE LYSIN DIMER==
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<StructureSection load='3lyn' size='340' side='right'caption='[[3lyn]], [[Resolution|resolution]] 1.70&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'>[[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>
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]] 1.7&#8491;</td></tr>
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<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>
{{STRUCTURE_3lyn|  PDB=3lyn  |  SCENE=  }}
</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.


===STRUCTURE OF GREEN ABALONE LYSIN DIMER===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lyn" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_10698629}}, adds the Publication Abstract to the page
*[[Lysin 3D structures|Lysin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10698629 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_10698629}}
__TOC__
 
</StructureSection>
==About this Structure==
3LYN is a 2 chains structure of sequences 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].
 
==Reference==
<ref group="xtra">PMID:10698629</ref><references group="xtra"/>
[[Category: Haliotis fulgens]]
[[Category: Haliotis fulgens]]
[[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 12:59:18 2009''

Latest revision as of 03:32, 28 December 2023

STRUCTURE OF GREEN ABALONE LYSIN DIMERSTRUCTURE OF GREEN ABALONE LYSIN DIMER

Structural highlights

3lyn is a 2 chain structure with sequence from Haliotis fulgens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

3lyn, resolution 1.70Å

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