2lyn: Difference between revisions
New page: left|200px<br /><applet load="2lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lyn, resolution 2.07Å" /> '''HIGH RESOLUTION STRU... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2lyn.gif|left|200px]]<br /><applet load="2lyn" size=" | [[Image:2lyn.gif|left|200px]]<br /><applet load="2lyn" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2lyn, resolution 2.07Å" /> | caption="2lyn, resolution 2.07Å" /> | ||
'''HIGH RESOLUTION STRUCTURE OF RED ABALONE LYSIN DIMER'''<br /> | '''HIGH RESOLUTION STRUCTURE OF RED ABALONE LYSIN DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
Abalone sperm use lysin to make a hole in the egg's protective vitelline | 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. | ||
==About this Structure== | ==About this Structure== | ||
2LYN 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:// | 2LYN 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2LYN OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kresge, N.]] | [[Category: Kresge, N.]] | ||
[[Category: Stout, C | [[Category: Stout, C D.]] | ||
[[Category: Vacquier, V | [[Category: Vacquier, V D.]] | ||
[[Category: abalone lysin]] | [[Category: abalone lysin]] | ||
[[Category: fertilization protein]] | [[Category: fertilization protein]] | ||
[[Category: gamete recognition protein]] | [[Category: gamete recognition protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:14 2008'' | ||
Revision as of 19:07, 21 February 2008
|
HIGH RESOLUTION STRUCTURE OF RED ABALONE LYSIN DIMER
OverviewOverview
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.
About this StructureAbout this Structure
2LYN is a Single protein structure of sequence from Haliotis rufescens. Full crystallographic information is available from OCA.
ReferenceReference
1.35 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
Page seeded by OCA on Thu Feb 21 18:07:14 2008