1lyn

From Proteopedia

(Difference between revisions)

Revision as of 06:50, 18 August 2021

CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES

Structural highlights

1lyn is a 2 chain structure with sequence from California red abalone. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:7657696^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shaw A, Fortes PA, Stout CD, Vacquier VD. Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species. J Cell Biol. 1995 Sep;130(5):1117-25. PMID:7657696

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lyn"

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/California_red_abalone California red abalone]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LYN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lyn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/California_red_abalone California red abalone]. 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyn OCA], [http://pdbe.org/1lyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lyn RCSB], [http://www.ebi.ac.uk/pdbsum/1lyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyn ProSAT]</span></td></tr>
+</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 ==
-[[http://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.
+[[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]]

1lyn

From Proteopedia

Revision as of 06:50, 18 August 2021

CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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