User:Cameron Evans/Sandbox 1: Difference between revisions
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Like most prokaryotic GluDH, Mammalian GluDH has been found to hexamerize as a dimer of | Like most prokaryotic GluDH, Mammalian GluDH has been found to hexamerize as a dimer of | ||
<scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/ | <scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/4'>trimers</scene>. | ||
Furthermore,each <scene name='User:Cameron_Evans/Sandbox_1/Human_d_alone/1'>monomer</scene> of mammalian GluDH, like prokaryotic GluDH, is composed of two domains: Domain I, which is responsible for the assembly of the hexamer; and Domain II, which is responsible for dinucleotide binding (both true statements for prokaryotic GluDH). Furthermore, each domain is similar to the domains within csGluDH as <scene name='User:Cameron_Evans/Sandbox_1/Bogdh_2ndary/1'>each is a beta sheet flanked by alpha helices</scene>. | Furthermore,each <scene name='User:Cameron_Evans/Sandbox_1/Human_d_alone/1'>monomer</scene> of mammalian GluDH, like prokaryotic GluDH, is composed of two domains: Domain I, which is responsible for the assembly of the hexamer; and Domain II, which is responsible for dinucleotide binding (both true statements for prokaryotic GluDH). Furthermore, each domain is similar to the domains within csGluDH as <scene name='User:Cameron_Evans/Sandbox_1/Bogdh_2ndary/1'>each is a beta sheet flanked by alpha helices</scene>. | ||
Unlike csGluDH, the boGluDH monomer has 48 residue <scene name='User:Cameron_Evans/Sandbox_1/Tail_1/1'>"antenna"</scene> that assists in the trimerization process. <scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/ | Unlike csGluDH, the boGluDH monomer has 48 residue <scene name='User:Cameron_Evans/Sandbox_1/Tail_1/1'>"antenna"</scene> that assists in the trimerization process. <scene name='User:Cameron_Evans/Sandbox_1/Human_d_e_f/6'>(The interactions of the antennae are best seen in the trimer)</scene>. These antennae appear to undergo conformational changes as the "mouth" of GluDH opens and closes. | ||
This 48 residue insertion (397-444), which does not exist in the sequences of prokaryotic GluDH, is thought to be significant for the allosteric interactions that distinguish mammalian GluDH from prokaryotic GluDH (see specific interactions below).<ref name=1hwx /> | This 48 residue insertion (397-444), which does not exist in the sequences of prokaryotic GluDH, is thought to be significant for the allosteric interactions that distinguish mammalian GluDH from prokaryotic GluDH (see specific interactions below).<ref name=1hwx /> | ||
