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='82/823087/Impdh_secondary_structure/1'>secondary structure</scene> shows alpha helices | The <scene name='82/823087/Impdh_secondary_structure/1'>secondary structure</scene> shows alpha helices and beta sheets. The ''Ashbya gossypii'' IMPDH is 31% helical and 15% beta sheet, which 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. | ||
IMPDH <scene name='82/823087/Impdh_quaternary_structure/1'>quaternary structures</scene> include multiunit complexes, such as tetramers, extended octamers, and compacted octamers. These quaternary structures are created through the binding of multiple subunits of tertiary structures, 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. | IMPDH <scene name='82/823087/Impdh_quaternary_structure/1'>quaternary structures</scene> include multiunit complexes, such as tetramers, extended octamers, and compacted octamers. These quaternary structures are created through the binding of multiple subunits of tertiary structures, 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. | ||
