Lysin: Difference between revisions
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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>. | 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>. | ||
== 3D structure of lysin == | |||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[1lis]], [[1lyn]], [[2lis]], [[2lyn]], [[3lyn]] – Lys - abalone<br /> | |||
[[1nkl]] – NK-Lys – pig – NMR<br /> | |||
[[4cvd]] – Lys – bacteriophage CP-7<br /> | |||
[[1h09]] – bLys – bacteriophage CP-1<br /> | |||
[[1oba]] – bLys + choline<br /> | |||
[[2ixu]] – bLys + peptidoglycan analog<br /> | |||
[[2ixv]], [[2j8f]], [[2j8g]] – bLys (mutant) + peptidoglycan analog<br /> | |||
[[2mk5]] – GH15Lys residues 368-495 – phage GH15 – NMR<br /> | |||
[[4olk]] – GH15Lys CHAP domain residues 1-165<br /> | |||
[[4ols]] – GH15Lys amidase domain residues 165-403<br /> | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:45, 31 January 2016
FunctionLysin (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. Structural highlightsThe structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. you can see the alpha helixes in pink. exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of ,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action[1]. 3D structure of lysinUpdated on 04-June-2025 1lis, 1lyn, 2lis, 2lyn, 3lyn – Lys - abalone 1nkl – NK-Lys – pig – NMR |
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