3lyn
From Proteopedia
(New page: 200px<br /><applet load="3lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lyn, resolution 1.70Å" /> '''STRUCTURE OF GREEN A...) |
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| - | [[Image:3lyn.jpg|left|200px]]<br /><applet load="3lyn" size=" | + | [[Image:3lyn.jpg|left|200px]]<br /><applet load="3lyn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3lyn, resolution 1.70Å" /> | caption="3lyn, resolution 1.70Å" /> | ||
'''STRUCTURE OF GREEN ABALONE LYSIN DIMER'''<br /> | '''STRUCTURE OF GREEN ABALONE LYSIN DIMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Abalone sperm lysin is a 16 kDa acrosomal protein used by sperm to create | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 3LYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haliotis_fulgens Haliotis fulgens]. Full crystallographic information is available from [http:// | + | 3LYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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== | ==Reference== | ||
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[[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 19:10:16 2008'' |
Revision as of 17:10, 21 February 2008
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STRUCTURE OF GREEN ABALONE LYSIN DIMER
Overview
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.
About this Structure
3LYN is a Single protein structure of sequence from Haliotis fulgens. Full crystallographic information is available from OCA.
Reference
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
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