3lyn: Difference between revisions

New page: left|200px<br /><applet load="3lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lyn, resolution 1.70Å" /> '''STRUCTURE OF GREEN A...
 
No edit summary
Line 1: Line 1:
[[Image:3lyn.jpg|left|200px]]<br /><applet load="3lyn" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:3lyn.jpg|left|200px]]<br /><applet load="3lyn" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="3lyn, resolution 1.70&Aring;" />
caption="3lyn, resolution 1.70&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=3LYN OCA].  
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==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kresge, N.]]
[[Category: Kresge, N.]]
[[Category: Stout, C.D.]]
[[Category: Stout, C D.]]
[[Category: Vacquier, V.D.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:49:52 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:16 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA