1b25: Difference between revisions
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|PDB= 1b25 |SIZE=350|CAPTION= <scene name='initialview01'>1b25</scene>, resolution 1.85Å | |PDB= 1b25 |SIZE=350|CAPTION= <scene name='initialview01'>1b25</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=PTT:TUNGSTOPTERIN'>PTT</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b25 OCA], [http://www.ebi.ac.uk/pdbsum/1b25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b25 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
[[Category: Roy, R.]] | [[Category: Roy, R.]] | ||
[[Category: hyperthermophile]] | [[Category: hyperthermophile]] | ||
[[Category: moco]] | [[Category: moco]] | ||
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[[Category: tungstoenzyme]] | [[Category: tungstoenzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:58 2008'' | ||
Revision as of 15:52, 30 March 2008
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| 1b25, resolution 1.85Å | |||||||||||||
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| Ligands: | PTT, SF4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS
Overview
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
1B25 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
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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