1b0p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b0p, resolution 2.31&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1b0p.gif|left|200px]]<br /><applet load="1b0p" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1b0p.gif|left|200px]]<br /><applet load="1b0p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b0p, resolution 2.31&Aring;" />
caption="1b0p, resolution 2.31&Aring;" />
'''CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS'''<br />
'''CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS'''<br />
==Overview==
==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==
==About this Structure==
-
1B0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio africanus] with MG, CA, SF4 and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B0P OCA].
+
1B0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_africanus Desulfovibrio africanus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=TPP:'>TPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0P OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chabriere, E.]]
[[Category: Chabriere, E.]]
-
[[Category: Charon, M.H.]]
+
[[Category: Charon, M H.]]
[[Category: Volbeda, A.]]
[[Category: Volbeda, A.]]
[[Category: CA]]
[[Category: CA]]
Line 26: Line 26:
[[Category: tpp-dependent enzyme]]
[[Category: tpp-dependent enzyme]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:34:30 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:17 2008''

Revision as of 09:50, 21 February 2008


1b0p, resolution 2.31Å

Drag the structure with the mouse to rotate

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 with , , and as ligands. Active as Pyruvate synthase, with EC number 1.2.7.1 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

Page seeded by OCA on Thu Feb 21 11:50:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools