2pda: Difference between revisions

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==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.

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==

Line 15:

[[Category: Single protein]]

[[Category: Chabriere, E.]]

[[Category: Charon, M.H.]]

[[Category: Charon, M H.]]

[[Category: CA]]

[[Category: MG]]

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[[Category: tpp-dependent enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29~~ 21:22~~:34~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:22 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Chabriere, E.]]
-[[Category: Charon, M.H.]]
+[[Category: Charon, M H.]]
 [[Category: CA]]
 [[Category: MG]]
@@ Line 27: / Line 27: @@
 [[Category: tpp-dependent enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:22:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:22 2008''