Sandbox Reserved 1565: Difference between revisions
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== Structural Highlights and Structure-Function Relationships == | == Structural Highlights and Structure-Function Relationships == | ||
The <scene name='82/823089/Secondary_structure/1'>secondary structure</scene> shows alpha helices and beta sheets. The ''Ashbya gossypii'' IMPDH is 31% helical and 15% beta sheet, with the other percentages including random coils and residue structures. The active site is located towards the C-terminus within the TIM barrel, containing 8 alpha-helices and 8 beta sheets. The CBS | The <scene name='82/823089/Secondary_structure/1'>secondary structure</scene> shows alpha helices and beta sheets. The ''Ashbya gossypii'' IMPDH is 31% helical and 15% beta sheet, with the other percentages including random coils and residue structures. The active site is located towards the C-terminus within the TIM barrel, containing 8 alpha-helices and 8 beta sheets. The CBS region is recognized in the secondary structure through its beta-alpha-beta-beta-alpha pattern -- IMPDH contains a CBS-pair (Bateman domain) that arranges two of these patterns together. | ||
IMPDH quaternary structures include multiunit complexes, such as <scene name='82/823089/Quaternary_view/1'>tetramers</scene>, extended octamers, and compacted octamers. These quaternary structures are created through the binding of multiple subunits of <scene name='82/823089/Tertiary_structure/1'>tertiary</scene> structures (monomers), that are strengthened and structurally formed through hydrogen-bonding, cysteine-cysteine disulfide bonds, and hydrophobic interactions. Different quaternary forms of IMPDH relate to the kinetic favorability of the IMPDH mechanism as Bateman domain allosteric binding sites and competitive nature changes with unit composition. The secondary structure of IMPDH's Bateman domain is folded, so its antiparallel beta-sheets are surrounded by the alpha helices (one on each side) to form a globular tertiary structure. | IMPDH quaternary structures include multiunit complexes, such as <scene name='82/823089/Quaternary_view/1'>tetramers</scene>, extended octamers, and compacted octamers. These quaternary structures are created through the binding of multiple subunits of <scene name='82/823089/Tertiary_structure/1'>tertiary</scene> structures (monomers), that are strengthened and structurally formed through hydrogen-bonding, cysteine-cysteine disulfide bonds, and hydrophobic interactions. Different quaternary forms of IMPDH relate to the kinetic favorability of the IMPDH mechanism as Bateman domain allosteric binding sites and competitive nature changes with unit composition. The secondary structure of IMPDH's Bateman domain is folded, so its antiparallel beta-sheets are surrounded by the alpha helices (one on each side) to form a globular tertiary structure. | ||
