1mjg

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(New page: 200px<br /><applet load="1mjg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjg, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF BIFUNCTIONAL CARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE(CODH/ACS) FROM MOORELLA THERMOACETICA (F. CLOSTRIDIUM THERMOACETICUM)'''<br />
'''CRYSTAL STRUCTURE OF BIFUNCTIONAL CARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE(CODH/ACS) FROM MOORELLA THERMOACETICA (F. CLOSTRIDIUM THERMOACETICUM)'''<br />
==Overview==
==Overview==
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A metallocofactor containing iron, sulfur, copper, and nickel has been, discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA, (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium, thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the, cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4], cubane bridged to a copper-nickel binuclear site. The presence of these, three metals together in one cluster was unanticipated and suggests a, newly discovered role for copper in biology. The different active sites of, this bifunctional enzyme complex are connected via a channel, 138, angstroms long, that provides a conduit for carbon monoxide generated at, the C-cluster on one subunit to be incorporated into acetyl-CoA at the, A-cluster on the other subunit.
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A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.
==About this Structure==
==About this Structure==
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1MJG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with CU1, NI, ACT, SF4 and XCC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MJG OCA].
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1MJG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica] with <scene name='pdbligand=CU1:'>CU1</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=XCC:'>XCC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJG OCA].
==Reference==
==Reference==
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[[Category: Moorella thermoacetica]]
[[Category: Moorella thermoacetica]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Doukov, T.I.]]
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[[Category: Doukov, T I.]]
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[[Category: Drennan, C.L.]]
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[[Category: Drennan, C L.]]
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[[Category: Iverson, T.M.]]
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[[Category: Iverson, T M.]]
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[[Category: Ragsdale, S.W.]]
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[[Category: Ragsdale, S W.]]
[[Category: Seravalli, J.]]
[[Category: Seravalli, J.]]
[[Category: ACT]]
[[Category: ACT]]
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[[Category: wood-ljundahl pathway]]
[[Category: wood-ljundahl pathway]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:27:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:45 2008''

Revision as of 11:55, 21 February 2008


1mjg, resolution 2.2Å

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CRYSTAL STRUCTURE OF BIFUNCTIONAL CARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE(CODH/ACS) FROM MOORELLA THERMOACETICA (F. CLOSTRIDIUM THERMOACETICUM)

Overview

A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.

About this Structure

1MJG is a Protein complex structure of sequences from Moorella thermoacetica with , , , and as ligands. Active as Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 Full crystallographic information is available from OCA.

Reference

A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase., Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL, Science. 2002 Oct 18;298(5593):567-72. PMID:12386327

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