2c3y
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2c3y |SIZE=350|CAPTION= <scene name='initialview01'>2c3y</scene>, resolution 1.93Å | |PDB= 2c3y |SIZE=350|CAPTION= <scene name='initialview01'>2c3y</scene>, resolution 1.93Å | ||
|SITE= <scene name='pdbsite=AC1:Co2+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Co2+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=HTL:2-ACETYL-THIAMINE+DIPHOSPHATE'>HTL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=2c3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3y OCA], [http://www.ebi.ac.uk/pdbsum/2c3y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c3y RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Hatchikian, E C.]] | [[Category: Hatchikian, E C.]] | ||
[[Category: Pieulle, L.]] | [[Category: Pieulle, L.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CO2]] | ||
| - | [[Category: HTL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SF4]] | ||
[[Category: 4fe-4]] | [[Category: 4fe-4]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| Line 44: | Line 42: | ||
[[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 Mon Mar 31 02:15:59 2008'' |
Revision as of 23:16, 30 March 2008
| |||||||
| , resolution 1.93Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| 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 THE RADICAL FORM OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS
Overview
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 inhibition of catalytic activity, both in solution and in the crystals. Examination of the crystal structure of inhibited PFOR suggests that the loss of activity results from oxime formation at the 4' amino substituent of the pyrimidine moiety of ThDP.
About this Structure
2C3Y is a Single protein structure of sequence from Desulfovibrio africanus. Full crystallographic information is available from OCA.
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:16472741
Page seeded by OCA on Mon Mar 31 02:15:59 2008
Categories: Desulfovibrio africanus | Pyruvate synthase | Single protein | Cavazza, C. | Chabriere, E. | Contreras-Martel, C. | Fontecilla-Camps, J C. | Hatchikian, E C. | Pieulle, L. | 4fe-4 | Electron transport | Iron | Iron-sulfur | Iron-sulfur cluster | Metal-binding | Oxidoreductase | Pyruvate catabolism | Tpp-dependent enzyme
