2c3p: Difference between revisions

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New page: left|200px<br /> <applet load="2c3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3p, resolution 2.33Å" /> '''CRYSTAL STRUCTURE O...
 
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==About this Structure==
==About this Structure==
2C3P 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 1TP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=2C3P OCA]].  
2C3P 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 1TP 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3P OCA]].  


==Reference==
==Reference==
Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate., Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC, Structure. 2006 Feb;14(2):217-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16472741 16472741]
Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate., Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC, Structure. 2006 Feb;14(2):217-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16472741 16472741]
[[Category: Desulfovibrio africanus]]
[[Category: Desulfovibrio africanus]]
[[Category: Pyruvate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cavazza, C.]]
[[Category: Cavazza, C.]]
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[[Category: tpp-dependent enzyme]]
[[Category: tpp-dependent enzyme]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:55:25 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:11:24 2007''

Revision as of 13:06, 30 October 2007

File:2c3p.gif


2c3p, resolution 2.33Å

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CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS

OverviewOverview

Pyruvate-ferredoxin oxidoreductases (PFOR) are unique among thiamine, pyrophosphate (ThDP)-containing enzymes in giving rise to a rather stable, cofactor-based free-radical species upon the decarboxylation of their, first substrate, pyruvate. We have obtained snapshots of unreacted and, partially reacted (probably as a tetrahedral intermediate) pyruvate-PFOR, complexes at different time intervals. We conclude that pyruvate, decarboxylation involves very limited substrate-to-product movements but a, significant displacement of the thiazolium moiety of ThDP. In this, respect, PFOR seems to differ substantially from other ThDP-containing, enzymes, such as transketolase and pyruvate decarboxylase. In addition, exposure of PFOR to oxygen in the presence of pyruvate results in, significant ... [(full description)]

About this StructureAbout this Structure

2C3P is a [Single protein] structure of sequence from [Desulfovibrio africanus] with MG, CA, SF4 and 1TP as [ligands]. Active as [Pyruvate synthase], with EC number [1.2.7.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate., Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC, Structure. 2006 Feb;14(2):217-24. PMID:16472741

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