View source for 2pda

[[Image:2pda.jpg|left|200px]]

 {{Structure
|PDB= 2pda |SIZE=350|CAPTION= <scene name='initialview01'>2pda</scene>, resolution 3.0&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</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] 
|GENE= 
}}

'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS AND PYRUVATE.'''


==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==
2PDA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio africanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDA 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:[http://www.ncbi.nlm.nih.gov/pubmed/10048931 10048931]
[[Category: Desulfovibrio africanus]]
[[Category: Pyruvate synthase]]
[[Category: Single protein]]
[[Category: Chabriere, E.]]
[[Category: Charon, M H.]]
[[Category: CA]]
[[Category: MG]]
[[Category: PYR]]
[[Category: SF4]]
[[Category: TPP]]
[[Category: complex]]
[[Category: iron-sulfur cluster]]
[[Category: oxidoreductase]]
[[Category: pyruvate catabolism]]
[[Category: tpp-dependent enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:11:45 2008''