Sandbox Reserved 1565: Difference between revisions

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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. The [6] beta-sheets of the <scene name='82/823089/Batemancbs/2'>Bateman domain</scene> swirl to form an opening, known as the TIM barrel (zoomed in, in image) with the [4] alpha helices surrounding the beta-sheet-forming tunnel. This CBS-pair (cystathionine beta synthase motif) allows for monocovalent cations to move through and activate IMPDH as amino acid residues in the active site interact with ligands.

This <scene name='82/823089/Space-filled/2'>space-filled view</scene> helps show the Van der Waals interactions and areas for movement within the structure. The ability for monovalent cations to move within the charged tunnel with the phosphate chain (TIM barrel) directly relates to activation levels. The phosphate chain relates to the ligands that further interact with the binding site to form the covalent intermediate, E-XMP*.

Sandbox Reserved 1565: Difference between revisions

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 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. The [6] beta-sheets of the <scene name='82/823089/Batemancbs/2'>Bateman domain</scene> swirl to form an opening, known as the TIM barrel (zoomed in, in image) with the [4] alpha helices surrounding the beta-sheet-forming tunnel. This CBS-pair (cystathionine beta synthase motif) allows for monocovalent cations to move through and activate IMPDH as amino acid residues in the active site interact with ligands.
 This <scene name='82/823089/Space-filled/2'>space-filled view</scene> helps show the Van der Waals interactions and areas for movement within the structure. The ability for monovalent cations to move within the charged tunnel with the phosphate chain (TIM barrel) directly relates to activation levels. The phosphate chain relates to the ligands that further interact with the binding site to form the covalent intermediate, E-XMP*.