This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lyn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lyn.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1lyn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lyn| PDB=1lyn | SCENE= }}
{{STRUCTURE_1lyn| PDB=1lyn | SCENE= }}
-
'''CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES'''
+
===CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7657696}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7657696 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7657696}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Vacquier, V D.]]
[[Category: Vacquier, V D.]]
[[Category: Fertilization protein]]
[[Category: Fertilization protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:25:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:49:53 2008''

Revision as of 19:49, 2 July 2008

Image:1lyn.png

Template:STRUCTURE 1lyn

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

Template:ABSTRACT PUBMED 7657696

About this Structure

1LYN is a Single protein structure of sequence from Haliotis rufescens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Wed Jul 2 22:49:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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