3lyn
From Proteopedia
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| - | [[Image:3lyn.jpg|left|200px]] | + | [[Image:3lyn.jpg|left|200px]] |
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| - | '''STRUCTURE OF GREEN ABALONE LYSIN DIMER''' | + | {{Structure |
| + | |PDB= 3lyn |SIZE=350|CAPTION= <scene name='initialview01'>3lyn</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF GREEN ABALONE LYSIN DIMER''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3LYN is a [ | + | 3LYN is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10698629 10698629] |
[[Category: Haliotis fulgens]] | [[Category: Haliotis fulgens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gamete recognition protein]] | [[Category: gamete recognition protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:05:48 2008'' |
Revision as of 17:05, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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