Sandbox Reserved 1475: Difference between revisions

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The structure was based on the mitochondrial aldehyde dehydrogenase type two. RalDH2 in a monomer made up of 3 domains: a nucleotide-binding domain (1-136, 161-270), a catalytic domain (271-484), and a tetramerization domain (137-160, 485-484) as shown in [[Figure 1]].<ref name="Lamb AL, Newcomber ME" />

The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" as seen in [[Figure 2]].<ref name="Lamb AL, Newcomber ME" /> The <scene name='80/800654/1st_dimerization/1'>1st dimerization</scene> is presented by the alpha1 helix and beta11 strand of one nucleotide-binding domain, with the same alpha1 helix and beta11 strand of it's dimer ([[Figure 2]], the purple highlighted region). Although the beta strands are far apart, ordered water molecules are present to create beta-sheet contacts.<ref name="Lamb AL, Newcomber ME" /> The ~~second dimerization interface~~ is presented by the beta18 of the catalytic domain beta-sheet of one monomer and the beta19 of the tetramerization domain of it's dimer.<ref name="Lamb AL, Newcomber ME" /> This dimerization interaction creates an "embrace" between the beta-sheet's contact, and creates a channel for the substrate to access the active site.<ref name="Lamb AL, Newcomber ME" />

The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" as seen in [[Figure 2]].<ref name="Lamb AL, Newcomber ME" /> The <scene name='80/800654/1st_dimerization/1'>1st dimerization</scene> is presented by the alpha1 helix and beta11 strand of one nucleotide-binding domain, with the same alpha1 helix and beta11 strand of it's dimer ([[Figure 2]], the purple highlighted region). Although the beta strands are far apart, ordered water molecules are present to create beta-sheet contacts.<ref name="Lamb AL, Newcomber ME" /> The <scene name='80/800654/2nd_dimerization/1'>2nd Dimerization</scene> is presented by the beta18 of the catalytic domain beta-sheet of one monomer and the beta19 of the tetramerization domain of it's dimer([[Figure 2]], the pink highlighted region).<ref name="Lamb AL, Newcomber ME" /> This dimerization interaction creates an "embrace" between the beta-sheet's contact, and creates a channel for the substrate to access the active site.<ref name="Lamb AL, Newcomber ME" />

In [[Figure 3]] it is possible to see the active site, which is where the substrate interacts with Cys-302.

Sandbox Reserved 1475: Difference between revisions

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 The structure was based on the mitochondrial aldehyde dehydrogenase type two. RalDH2 in a monomer made up of 3 domains: a nucleotide-binding domain (1-136, 161-270), a catalytic domain (271-484), and a tetramerization domain (137-160, 485-484) as shown in [[Figure 1]].<ref name="Lamb AL, Newcomber ME" />
-The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" as seen in [[Figure 2]].<ref name="Lamb AL, Newcomber ME" />  The <scene name='80/800654/1st_dimerization/1'>1st dimerization</scene> is presented by the alpha1 helix and beta11 strand of one nucleotide-binding domain, with the same alpha1 helix and beta11 strand of it's dimer ([[Figure 2]], the purple highlighted region).  Although the beta strands are far apart, ordered water molecules are present to create beta-sheet contacts.<ref name="Lamb AL, Newcomber ME" /> The second dimerization interface is presented by the beta18 of the catalytic domain beta-sheet of one monomer and the beta19 of the tetramerization domain of it's dimer.<ref name="Lamb AL, Newcomber ME" /> This dimerization interaction creates an "embrace" between the beta-sheet's contact, and creates a channel for the substrate to access the active site.<ref name="Lamb AL, Newcomber ME" />
+The tetramer can be envisioned as an "X", with nucleotide-binding sites at the tips of the "X", and the tetramerization domains as the equatorial portion of the "X" as seen in [[Figure 2]].<ref name="Lamb AL, Newcomber ME" />  The <scene name='80/800654/1st_dimerization/1'>1st dimerization</scene> is presented by the alpha1 helix and beta11 strand of one nucleotide-binding domain, with the same alpha1 helix and beta11 strand of it's dimer ([[Figure 2]], the purple highlighted region).  Although the beta strands are far apart, ordered water molecules are present to create beta-sheet contacts.<ref name="Lamb AL, Newcomber ME" /> The <scene name='80/800654/2nd_dimerization/1'>2nd Dimerization</scene> is presented by the beta18 of the catalytic domain beta-sheet of one monomer and the beta19 of the tetramerization domain of it's dimer([[Figure 2]], the pink highlighted region).<ref name="Lamb AL, Newcomber ME" /> This dimerization interaction creates an "embrace" between the beta-sheet's contact, and creates a channel for the substrate to access the active site.<ref name="Lamb AL, Newcomber ME" />
 In [[Figure 3]] it is possible to see the active site, which is where the substrate interacts with Cys-302.