Sandbox Reserved 496

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==='''Mechanism of Action'''===
==='''Mechanism of Action'''===
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There are two proposed mechanisms for the catalytic action of the A-cluster.
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There are two proposed mechanisms for the catalytic action of the A-cluster <ref name="Cu"/> <ref name="Zn">PMID:12627225</ref>.
[[Image:A_cluster_1.JPG|frame|Proposed mechanism for ACS activity with Cu-Ni ions in the binuclear site of the A-cluster.]] [[Image:A_cluster_2.JPG|frame|Proposed mechanism for ACS activity with Ni-Ni ions in the binuclear site of the A-cluster.]]
[[Image:A_cluster_1.JPG|frame|Proposed mechanism for ACS activity with Cu-Ni ions in the binuclear site of the A-cluster.]] [[Image:A_cluster_2.JPG|frame|Proposed mechanism for ACS activity with Ni-Ni ions in the binuclear site of the A-cluster.]]
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Proposed catalytic action of the C-cluster.
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Proposed catalytic action of the C-cluster <ref name="CN">PMID:19583207</ref>.
[[Image:C_cluster.JPG|frame|Proposed mechanism for CODH activity in the C-cluster.]]
[[Image:C_cluster.JPG|frame|Proposed mechanism for CODH activity in the C-cluster.]]
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==='''Possible Applications'''===
==='''Possible Applications'''===
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Revision as of 01:40, 2 May 2012

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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.

Drag the structure with the mouse to rotate


Introduction

PDB codes for the M. thermoacetica enzyme are: 1MJG [1] (shown at right), 1OAO [2], 2Z8Y [3], 3I01 [4], and 3I04 [5].

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


Mechanism of Action

There are two proposed mechanisms for the catalytic action of the A-cluster [6] [7].

Proposed mechanism for ACS activity with Cu-Ni ions in the binuclear site of the A-cluster.
Proposed mechanism for ACS activity with Cu-Ni ions in the binuclear site of the A-cluster.
Proposed mechanism for ACS activity with Ni-Ni ions in the binuclear site of the A-cluster.
Proposed mechanism for ACS activity with Ni-Ni ions in the binuclear site of the A-cluster.

Proposed catalytic action of the C-cluster [8].

Proposed mechanism for CODH activity in the C-cluster.
Proposed mechanism for CODH activity in the C-cluster.

Possible Applications


References

  1. ↑ 1MJG. DOI:10.2210/pdb1mjg/pdb
  2. ↑ 1OAO. DOI:10.2210/pdb1oao/pdb
  3. ↑ 2Z8Y. DOI:10.2210/pdb2z8y/pdb
  4. ↑ 3I01. DOI:10.2210/pdb3i01/pdb
  5. ↑ 3I04. DOI:10.2210/pdb3i04/pdb
  6. ↑ 6.0 6.1 Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science. 2002 Oct 18;298(5593):567-72. PMID:12386327 doi:10.1126/science.1075843
  7. ↑ Darnault C, Volbeda A, Kim EJ, Legrand P, Vernede X, Lindahl PA, Fontecilla-Camps JC. Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat Struct Biol. 2003 Apr;10(4):271-9. PMID:12627225 doi:10.1038/nsb912
  8. ↑ Kung Y, Doukov TI, Seravalli J, Ragsdale SW, Drennan CL. Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 2009 Jul 7. PMID:19583207 doi:10.1021/bi900574h
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