Sandbox Reserved 761: Difference between revisions

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==Glutamate Dehydrogenase Structure==

GDH is a homohexamer of 505 residues with a molecular weight of 55.638 KDa <ref>http://www.rcsb.org/pdb</ref>. The overall <scene name='56/564037/Secondary_structures/1'>secondary structures</scene> of GDH is composed of eighteen '''alpha helices''' and thirteen '''beta strands''', which are both parallel and anti-parallel and flanked by a layer of alpha helices <ref>http://www.rcsb.org/pdb</ref>.

GDH is a homohexamer of 505 residues with a molecular weight of 55.638 KDa <ref>http://www.rcsb.org/pdb</ref>. The overall <scene name='56/564037/Secondary_structures/1'>secondary structures</scene> of GDH is composed of eighteen '''alpha helices''' and thirteen '''beta strands''', which are both parallel and anti-parallel and flanked by a layer of alpha helices set in a 3-axis fold <ref>http://www.rcsb.org/pdb</ref>.

The monomer unit of GDH is essentially two trimers of six identical subunits containing <scene name='56/564037/Domains/1'>two distinct domains</scene>—the Glutamate (Glu) binding domain at the N terminus and the NAD binding doman—and a 48-residue antenna-like projection that extends from the top of each NAD binding domain, separated by a large active site cleft <ref>PMID:11258921</ref>. This 48-residue antenna consists of an ascending helix and a descending random coil strand that contains a small α-helix toward the C-terminal end of the strand. Domain I,also called the C-domain, is made up of residues 4-181 and 400-421, and is responsible for directing the assembly of the subunits into a hexamer. Domain II, also called the N-domain, makes up the glutamate-binding domain, and is composed of mainly beta sheets involving residues 182-399. <ref>PMID:16285734</ref>. <ref>PMID:11258921</ref>.

Sandbox Reserved 761: Difference between revisions

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@@ Line 15: / Line 15: @@
 ==Glutamate Dehydrogenase Structure==
-GDH is a homohexamer of 505 residues with a molecular weight of 55.638 KDa <ref>http://www.rcsb.org/pdb</ref>. The overall <scene name='56/564037/Secondary_structures/1'>secondary structures</scene> of GDH is composed of eighteen <font color="#ff0080">'''alpha helices'''</font> and thirteen <font color="#d0a000">'''beta strands'''</font>, which are both parallel and anti-parallel and flanked by a layer of alpha helices <ref>http://www.rcsb.org/pdb</ref>.
+GDH is a homohexamer of 505 residues with a molecular weight of 55.638 KDa <ref>http://www.rcsb.org/pdb</ref>. The overall <scene name='56/564037/Secondary_structures/1'>secondary structures</scene> of GDH is composed of eighteen <font color="#ff0080">'''alpha helices'''</font> and thirteen <font color="#d0a000">'''beta strands'''</font>, which are both parallel and anti-parallel and flanked by a layer of alpha helices set in a 3-axis fold <ref>http://www.rcsb.org/pdb</ref>.
 The monomer unit of GDH is essentially two trimers of six identical subunits containing <scene name='56/564037/Domains/1'>two distinct domains</scene>—the Glutamate (Glu) binding domain at the N terminus and the NAD binding doman—and a 48-residue antenna-like projection that extends from the top of each NAD binding domain, separated by a large active site cleft <ref>PMID:11258921</ref>. This 48-residue antenna consists of an ascending helix and a descending random coil strand that contains a small α-helix toward the C-terminal end of the strand. Domain I,also called the C-domain, is made up of residues 4-181 and 400-421, and is responsible for directing the assembly of the subunits into a hexamer.  Domain II, also called the N-domain, makes up the glutamate-binding domain, and is composed of mainly beta sheets involving residues 182-399. <ref>PMID:16285734</ref>. <ref>PMID:11258921</ref>.