2c42: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0p|1b0p]], [[1kek|1kek]], [[2pda|2pda]], [[2c3m|2c3m]], [[2c3o|2c3o]], [[2c3p|2c3p]], [[2c3u|2c3u]], [[2c3y|2c3y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0p|1b0p]], [[1kek|1kek]], [[2pda|2pda]], [[2c3m|2c3m]], [[2c3o|2c3o]], [[2c3p|2c3p]], [[2c3u|2c3u]], [[2c3y|2c3y]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c42 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c42 RCSB], [http://www.ebi.ac.uk/pdbsum/2c42 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c42 OCA], [http://pdbe.org/2c42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c42 RCSB], [http://www.ebi.ac.uk/pdbsum/2c42 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/P94692_DESAF P94692_DESAF]] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity).[PIRNR:PIRNR000159] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2c42" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 19:00, 10 September 2015
Crystal Structure Of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio africanusCrystal Structure Of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio africanus
Structural highlights
Function[P94692_DESAF] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (By similarity).[PIRNR:PIRNR000159] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPyruvate-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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