Sandbox 156: Difference between revisions

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[[Image:512px-Acetyl-CoA-2D.svg.png|thumb|300x1000 px|right|Structure of Acetyl-CoA]]

The general structure of CAT III is dominated by a six stranded antiparallel <scene name='Sandbox_156/Scene_4/4'>β-sheet</scene> and 5 <scene name='Sandbox_156/Scene_4/3'>α-helices</scene> stacked against the ends and face of the protein, forming a structure known as an "open-faced sandwhich"<ref>PMID: 3288984</ref>. Three identical monomers associate to form the trimeric protein with two <scene name='Sandbox_156/Scene_7/1'>cobalt</scene> ions acting as [http://en.wikipedia.org/wiki/Cofactor_%28biochemistry%29 cofactors].

The general structure of CAT III is dominated by a six stranded antiparallel <scene name='Sandbox_156/Scene_4/4'>β-sheet</scene> and 5 <scene name='Sandbox_156/Scene_4/3'>α-helices</scene> stacked against the ends and face of the protein, forming a structure known as an "open-faced sandwhich"<ref>PMID: 3288984</ref>. An extended β-strand forms an extension of the six stranded sheet to a seven stranded sheet that spans the interface of the subunit. Three identical monomers associate to form the trimeric protein with two <scene name='Sandbox_156/Scene_7/1'>cobalt</scene> ions acting as [http://en.wikipedia.org/wiki/Cofactor_%28biochemistry%29 cofactors].

===The Chloramphenicol Binding Site===

Sandbox 156: Difference between revisions

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@@ Line 22: / Line 22: @@
 <applet load='4CLA' size='300' frame='true' align='right' caption='' />
 [[Image:512px-Acetyl-CoA-2D.svg.png|thumb|300x1000 px|right|Structure of Acetyl-CoA]]
-The general structure of CAT III is dominated by a six stranded antiparallel <scene name='Sandbox_156/Scene_4/4'>β-sheet</scene> and 5 <scene name='Sandbox_156/Scene_4/3'>α-helices</scene> stacked against the ends and face of the protein, forming a structure known as an "open-faced sandwhich"<ref>PMID: 3288984</ref>. Three identical monomers associate to form the trimeric protein with two <scene name='Sandbox_156/Scene_7/1'>cobalt</scene> ions acting as [http://en.wikipedia.org/wiki/Cofactor_%28biochemistry%29 cofactors].
+The general structure of CAT III is dominated by a six stranded antiparallel <scene name='Sandbox_156/Scene_4/4'>β-sheet</scene> and 5 <scene name='Sandbox_156/Scene_4/3'>α-helices</scene> stacked against the ends and face of the protein, forming a structure known as an "open-faced sandwhich"<ref>PMID: 3288984</ref>. An extended β-strand forms an extension of the six stranded sheet to a seven stranded sheet that spans the interface of the subunit.  Three identical monomers associate to form the trimeric protein with two <scene name='Sandbox_156/Scene_7/1'>cobalt</scene> ions acting as [http://en.wikipedia.org/wiki/Cofactor_%28biochemistry%29 cofactors].
 ===The Chloramphenicol Binding Site===