1b0p
From Proteopedia
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|PDB= 1b0p |SIZE=350|CAPTION= <scene name='initialview01'>1b0p</scene>, resolution 2.31Å | |PDB= 1b0p |SIZE=350|CAPTION= <scene name='initialview01'>1b0p</scene>, resolution 2.31Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_synthase Pyruvate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_synthase Pyruvate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.1 1.2.7.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0p OCA], [http://www.ebi.ac.uk/pdbsum/1b0p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0p RCSB]</span> | ||
}} | }} | ||
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[[Category: Charon, M H.]] | [[Category: Charon, M H.]] | ||
[[Category: Volbeda, A.]] | [[Category: Volbeda, A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SF4]] | ||
| - | [[Category: TPP]] | ||
[[Category: iron-sulfur cluster]] | [[Category: iron-sulfur cluster]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| Line 35: | Line 34: | ||
[[Category: tpp-dependent enzyme]] | [[Category: tpp-dependent enzyme]] | ||
| - | ''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 18:51:21 2008'' |
Revision as of 15:51, 30 March 2008
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| , resolution 2.31Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Pyruvate synthase, with EC number 1.2.7.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
Overview
Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial step in many metabolic pathways, is carried out in most aerobic organisms by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design against certain anaerobic pathogens. Here, we report the crystal structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A resolution), and of its complex with pyruvate (3.0 A resolution). The structures show that each subunit consists of seven domains, one of which affords protection against oxygen. The thiamin pyrophosphate (TPP) cofactor and the three [4Fe-4S] clusters are suitably arranged to provide a plausible electron transfer pathway. In addition, the PFOR-pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction.
About this Structure
1B0P is a Single protein structure of sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate., Chabriere E, Charon MH, Volbeda A, Pieulle L, Hatchikian EC, Fontecilla-Camps JC, Nat Struct Biol. 1999 Feb;6(2):182-90. PMID:10048931
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