Lysin: Difference between revisions

← Older edit

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

Carmit Ginesin, Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

@@ Line 1: / Line 1: @@
-==egg lysin ==
+<StructureSection load='' size='340' side='right' caption='Abalone lysin (PDB code [[1lis]])' scene='60/607850/Lysin_fertilization_protein/1'>
-<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><scene name='60/607850/Alpha_helixes/1'>push here to see Lysine structure</scene>
 == Function ==
-Egg  Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg.
+'''Lysin''' (Lys) is a protein which cleaves cell walls.  Egg  Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg.
-== Relevance ==
+== Structural highlights ==
+The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. <scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action<ref>PMID:8266073</ref>.
-== Structural highlights ==
+== 3D structure of lysin ==
-The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule<scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.
+[[Lysin 3D structures]]
 </StructureSection>
 == References ==
 <references/>
-The crystal structure of lysin, a fertilization protein.
+[[Category:Topic Page]]
-Shaw A1, McRee DE, Vacquier VD, Stout CD.