1b25: Difference between revisions
New page: left|200px<br /><applet load="1b25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b25, resolution 1.85Å" /> '''FORMALDEHYDE FERREDO... |
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[[Image:1b25.gif|left|200px]]<br /><applet load="1b25" size=" | [[Image:1b25.gif|left|200px]]<br /><applet load="1b25" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1b25, resolution 1.85Å" /> | caption="1b25, resolution 1.85Å" /> | ||
'''FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS'''<br /> | '''FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a | Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a tungstopterin-containing protein from the hyperthermophilic archaeon Pyrococcus furiosus, have been determined in the native state and as a complex with the inhibitor glutarate at 1.85 A and 2. 4 A resolution, respectively. The native structure was solved by molecular replacement using the structure of the homologous P. furiosus aldehyde ferredoxin oxidoreductase (AOR) as the initial model. Residues are identified in FOR that may be involved in either the catalytic mechanism or in determining substrate specificity. The binding site on FOR for the physiological electron acceptor, P. furiosus ferredoxin (Fd), has been established from an FOR-Fd cocrystal structure. Based on the arrangement of redox centers in this structure, an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe:4S) cluster of FOR via one of the two pterins that coordinate the tungsten, and ends at the (4Fe:4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe:4S) clusters, Cys287 of FOR and Asp14 of ferredoxin. Similarities in the active site structures between FOR and the unrelated molybdoenzyme aldehyde oxidoreductase from Desulfovibrio gigas suggest that both enzymes utilize a common mechanism for aldehyde oxidation. | ||
==About this Structure== | ==About this Structure== | ||
1B25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with SF4 and PTT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1B25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=PTT:'>PTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B25 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adams, M | [[Category: Adams, M W.W.]] | ||
[[Category: Faham, S.]] | [[Category: Faham, S.]] | ||
[[Category: Hu, Y | [[Category: Hu, Y L.]] | ||
[[Category: Rees, D | [[Category: Rees, D C.]] | ||
[[Category: Roy, R.]] | [[Category: Roy, R.]] | ||
[[Category: PTT]] | [[Category: PTT]] | ||
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[[Category: tungstoenzyme]] | [[Category: tungstoenzyme]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:39 2008'' | ||
Revision as of 12:50, 21 February 2008
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FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS
OverviewOverview
Crystal structures of formaldehyde ferredoxin oxidoreductase (FOR), a tungstopterin-containing protein from the hyperthermophilic archaeon Pyrococcus furiosus, have been determined in the native state and as a complex with the inhibitor glutarate at 1.85 A and 2. 4 A resolution, respectively. The native structure was solved by molecular replacement using the structure of the homologous P. furiosus aldehyde ferredoxin oxidoreductase (AOR) as the initial model. Residues are identified in FOR that may be involved in either the catalytic mechanism or in determining substrate specificity. The binding site on FOR for the physiological electron acceptor, P. furiosus ferredoxin (Fd), has been established from an FOR-Fd cocrystal structure. Based on the arrangement of redox centers in this structure, an electron transfer pathway is proposed that begins at the tungsten center, leads to the (4Fe:4S) cluster of FOR via one of the two pterins that coordinate the tungsten, and ends at the (4Fe:4S) cluster of ferredoxin. This pathway includes two residues that coordinate the (4Fe:4S) clusters, Cys287 of FOR and Asp14 of ferredoxin. Similarities in the active site structures between FOR and the unrelated molybdoenzyme aldehyde oxidoreductase from Desulfovibrio gigas suggest that both enzymes utilize a common mechanism for aldehyde oxidation.
About this StructureAbout this Structure
1B25 is a Single protein structure of sequence from Pyrococcus furiosus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications., Hu Y, Faham S, Roy R, Adams MW, Rees DC, J Mol Biol. 1999 Feb 26;286(3):899-914. PMID:10024458
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