Sandbox 36: Difference between revisions

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===Secondary Structure===
===Secondary Structure===
''Gallus gallus'' egg white lysozyme has an alpha+beta fold, consisting of five to seven alpha helices and a three-stranded antiparallel beta sheet. There is also and a large amount of random coil and beta turns. The enzyme is approximately ellipsoidal in shape, with a large cleft in one side forming the active site. The openness of the secondary representation does not allow cleft identification. Click <scene name='Sandbox_36/Secondary/3'>view</scene> to visualize the cartoon portrayal of the enzyme with alpha helices and beta sheets highlighted. Click <scene name='Sandbox_36/Secondary/5'>view</scene> for the rainbow color ordered cartoon chain from N-C terminal.
''Gallus gallus'' egg white lysozyme has an alpha+beta fold, consisting of seven alpha helices and a three-stranded antiparallel beta sheet. There is also and a large amount of random coil and beta turns. The enzyme is approximately ellipsoidal in shape, with a large cleft in one side forming the active site. The openness of the secondary representation does not allow cleft identification. Click <scene name='Sandbox_36/Secondary/3'>view</scene> to visualize the cartoon portrayal of the enzyme with alpha helices and beta sheets highlighted. The alpha helix are highlighted in green and the beta sheets in clue. Click <scene name='Sandbox_36/Secondary/5'>view</scene> for the rainbow color ordered cartoon chain from N-C terminal.


<applet load='3IJU'' size='300' frame='true' align='right' caption='Egg White Lysozyme ' />
<applet load='3IJU'' size='300' frame='true' align='right' caption='Egg White Lysozyme ' />


==Function==
==Function==
Lysozyme’s main function is to protect from infection. The enzyme is a general non-specific organism defense effective against gram positive bacterial cells.  Lysozyme degrades the polysaccharides found in cells walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins<ref>Lysozyme. (2008). Retrieved from http://lysozyme.co.uk/</ref>. X-ray crystallography has shown that the binding of lysozyme and the substrates slightly deforms both structures. The binding first distorts the fourth hexose in the chain to the half chair conformation <ref>Voet, D, G., J, & W., C. (2008). Fundamentals of biochemistry: life at the molecular level. John Wiley & Sons Inc</ref>.  This imposes a strain on the C-O bond on the ring-4 side of the oxygen bridge between rings 4 and 5<ref> http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Enzymes.html#lysozyme </ref>. The polysaccharide is broken at this point and a molecule of water is inserted between the two hexoses. The reaction mechanism is shown below.
[[Image:Lys.gif]]
[[Image:Lys.gif]]