Sandbox Reserved 496

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This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Contents

Bifunctional Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase (CODH/ACS)

Carbon monoxide dehydrogenase/acetyl-CoA synthase asymmetric unit containing two α2β2 tetramers.

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Introduction


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. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands.


Mechanism of Action


Possible Applications


References
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