Sandbox Reserved 496: Difference between revisions
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=== '''Introduction''' === | === '''Introduction''' === | ||
---- | ---- | ||
PDB codes for the ''M. thermoacetica'' enzyme are: 1MJG <ref>IMJG. [http://dx.doi.org/10.2210/pdb1mjg/pdb DOI:10.2210/pdb1mjg/pdb]</ref> (shown at right), 1OAO, 2Z8Y, 3I01, and 3I04. | |||
==='''Structure'''=== | ==='''Structure'''=== | ||
---- | ---- | ||
The CODH/ACS enzyme from M. thermoacetica is an α2β2 tetramer. Each β subunit (residues 2 to 674) carries out CODH activity, while each α subunit (residues 2 to 729) is responsible for ACS activity. The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is comprised of three domains, two with α+β folds and a third with a helical region at the NH2-terminus of a Rossmann fold which is similar to a portion of the β subunit structure <ref name="Cu">PMID:12386327</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. Each β subunit (residues 2 to 674) carries out CODH activity, while each α subunit (residues 2 to 729) is responsible for ACS activity. The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. The α subunit is comprised of three domains, two with α+β folds and a third with a helical region at the NH2-terminus of a Rossmann fold which is similar to a portion of the β subunit structure <ref name="Cu">PMID:12386327</ref>. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands. | ||
==='''Mechanism of Action'''=== | ==='''Mechanism of Action'''=== | ||
