Sandbox Reserved 761: Difference between revisions
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==Glutamate Dehydrogenase Structure== | ==Glutamate Dehydrogenase Structure== | ||
GDH is a homohexamer of 505 residues with a molecular weight of 56 KDa (18 | GDH is a homohexamer of 505 residues with a molecular weight of 56 KDa (18). 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 (18) | ||
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, separated by a large active site cleft (9). | |||
[[Image:GDH1.jpg|frame|left|Figure 1. Each domain is colored differently - Glu-BD, NAD(P)-BD, antenna, the pivot helix. The allosteric regulators are shown as sphere models. This particular structure of GLUD1 is a combination of two X-ray structures - one with a bound GTP (1HWZ) and the second one with a bound ADP (1NQT). Although not real, this structure shows the relative position of the allosteric effectors when bound to GLUD1. NADPH and Glu are shown as well.]] | [[Image:GDH1.jpg|frame|left|Figure 1. Each domain is colored differently - Glu-BD, NAD(P)-BD, antenna, the pivot helix. The allosteric regulators are shown as sphere models. This particular structure of GLUD1 is a combination of two X-ray structures - one with a bound GTP (1HWZ) and the second one with a bound ADP (1NQT). Although not real, this structure shows the relative position of the allosteric effectors when bound to GLUD1. NADPH and Glu are shown as well.]] | ||
