Sandbox Reserved 1475: Difference between revisions

Line 17:

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" /> [[Image:3 Domains of RalDH2.png|thumb|upright=2| [[Figure 1]] Nucleotide-binding domain - orange, Catalytic domain - green, Tetramerization domain - blue. Imagine modified in Chimera from (PDB entry [[1bi9]]). Chain D shown with NAD substrate shown in pink]]

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

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

[[Image:Figure 3.png|thumb|upright=2| [[Figure 3]] Section (a) is the dimer of RalDH2 with the green spheres representing the amino and carboy termini of the substrate access channel loop. Section (b) shows the same orientation as section (a) with both dimers present and then the two dimers spun 90 degrees on the X-axis]]

</StructureSection>

Sandbox Reserved 1475: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 17: / Line 17: @@
 <Structure load='1bi9' size='350' frame='true' align='left' caption='[[Figure 2]] Nucleotide-Binding domain - orange, Catalytic domain - green, Tetramerization domain - blue (PDB entry [[1bi9]])' scene='80/800654/3_domains/3' />
 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" /> [[Image:3 Domains of RalDH2.png|thumb|upright=2| [[Figure 1]] Nucleotide-binding domain - orange, Catalytic domain - green, Tetramerization domain - blue. Imagine modified in Chimera from (PDB entry [[1bi9]]). Chain D shown with NAD substrate shown in pink]]
-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" /> In [[Figure 3]] it is possible to see the active site, which is where the substrate interacts with Cys-302.
+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" />  In [[Figure 3]] it is possible to see the active site, which is where the substrate interacts with Cys-302.
 [[Image:Figure 3.png|thumb|upright=2| [[Figure 3]] Section (a) is the dimer of RalDH2 with the green spheres representing the amino and carboy termini of the substrate access channel loop. Section (b) shows the same orientation as section (a) with both dimers present and then the two dimers spun 90 degrees on the X-axis]]
 </StructureSection>