Sandbox Reserved 1475: Difference between revisions
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==Retinal Dehydrogenase Type Two Structure== | ==Retinal Dehydrogenase Type Two Structure== | ||
<Structure load='1BI9' size=' | <Structure load='1BI9' size='200' frame='true' align='right' caption='Retinal Dehydrogenase Type Two with NAD bound (PDB entry [[1bi9]])' scene=" /> | ||
This molecular structure is Retinal Dehydrogenase Type Two (RalDH2). This enzyme is part of the super family Aldehyde Dehydrogenase. The function of this enzyme is to catalyze the oxidation of retinal to retinoic acid. Retinoic acid produces a putative morphogen that initiates pattern formation in the early embryo.<ref name="Lamb AL, Newcomber ME">PMID:10320326</ref> This is the last step in the formation of the hormone from Vitamin A (retinol).<ref name="Lamb AL, Newcomber ME" /> Vitamin A that has been metabolized can produce retinoid derivatives which function in either vision or growth and development. <ref name ="Families of Retinoic Dehydrogenases" /> RalDH2 is expressed in ''Escherichia coli'' strain BL21(DE3) <ref name=Lamb Al, Wang X>PMID:9761861</ref> | This molecular structure is Retinal Dehydrogenase Type Two (RalDH2). This enzyme is part of the super family Aldehyde Dehydrogenase. The function of this enzyme is to catalyze the oxidation of retinal to retinoic acid. Retinoic acid produces a putative morphogen that initiates pattern formation in the early embryo.<ref name="Lamb AL, Newcomber ME">PMID:10320326</ref> This is the last step in the formation of the hormone from Vitamin A (retinol).<ref name="Lamb AL, Newcomber ME" /> Vitamin A that has been metabolized can produce retinoid derivatives which function in either vision or growth and development. <ref name ="Families of Retinoic Dehydrogenases" /> RalDH2 is expressed in ''Escherichia coli'' strain BL21(DE3) <ref name=Lamb Al, Wang X>PMID:9761861</ref> | ||
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== Structural highlights == | == Structural highlights == | ||
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 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". | 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" (Figure 2). <Structure load='1bi9' size='350' frame='true' align='right' caption='' scene='' /> | ||
<Structure load=' | |||
