Sandbox Reserved 496: Difference between revisions

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==='''Structure'''===

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The CODH/ACS enzyme from ''M. thermoacetica'' is an α2β2 tetramer with seven metalloclusters. Each 674 residue β subunit carries out CODH activity, while each 729 residue α subunit is responsible for ACS activity. From the N- terminus to C-terminus, the domains of the β subunit are as follows: an α-helical domain (residues 1-257) followed by two α/β Rossmann-like domains (residues 262-458 and 463-674). The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is also comprised of three domains, two with α+β folds and a third with a helical region (residues 1-154) at the N-terminus of a Rossmann (six-stranded α/β) fold (residues 155-316) which is similar to a portion of the β subunit structure <ref name="Cu"/> <ref name="Xe">PMID:18293927</ref>. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.

The CODH/ACS enzyme from ''M. thermoacetica'' is an α2β2 tetramer with seven metalloclusters. Each 674 residue <scene name='Sandbox_Reserved_496/Beta_subunits/1'>β subunit</scene> β subunit carries out CODH activity, while each 729 residue α subunit is responsible for ACS activity. From the N- terminus to C-terminus, the domains of the β subunit are as follows: an α-helical domain (residues 1-257) followed by two α/β Rossmann-like domains (residues 262-458 and 463-674). The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is also comprised of three domains, two with α+β folds and a third with a helical region (residues 1-154) at the N-terminus of a Rossmann (six-stranded α/β) fold (residues 155-316) which is similar to a portion of the β subunit structure <ref name="Cu"/> <ref name="Xe">PMID:18293927</ref>. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.

Sandbox Reserved 496: Difference between revisions

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 ==='''Structure'''===
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-The CODH/ACS enzyme from ''M. thermoacetica'' is an α2β2 tetramer with seven metalloclusters.  Each 674 residue β subunit carries out CODH activity, while each 729 residue α subunit is responsible for ACS activity.  From the N- terminus to C-terminus, the domains of the β subunit are as follows: an α-helical domain (residues 1-257) followed by two α/β Rossmann-like domains (residues 262-458 and 463-674). The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is also comprised of three domains, two with α+β folds and a third with a helical region (residues 1-154) at the N-terminus of a Rossmann (six-stranded α/β) fold (residues 155-316) which is similar to a portion of the β subunit structure <ref name="Cu"/> <ref name="Xe">PMID:18293927</ref>.  Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.
+The CODH/ACS enzyme from ''M. thermoacetica'' is an α2β2 tetramer with seven metalloclusters. Each 674 residue <scene name='Sandbox_Reserved_496/Beta_subunits/1'>β subunit</scene>  β subunit carries out CODH activity, while each 729 residue α subunit is responsible for ACS activity.  From the N- terminus to C-terminus, the domains of the β subunit are as follows: an α-helical domain (residues 1-257) followed by two α/β Rossmann-like domains (residues 262-458 and 463-674). The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is also comprised of three domains, two with α+β folds and a third with a helical region (residues 1-154) at the N-terminus of a Rossmann (six-stranded α/β) fold (residues 155-316) which is similar to a portion of the β subunit structure <ref name="Cu"/> <ref name="Xe">PMID:18293927</ref>.  Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.