5c4i

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Revision as of 16:29, 15 November 2017

Structure of an Oxalate Oxidoreductase

Structural highlights

5c4i is a 6 chain structure with sequence from Moorella thermoacetica and Moorella thermoacetica (strain atcc 39073). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Activity:	Oxalate oxidoreductase, with EC number 1.2.7.10
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OORA_MOOTA] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.^[1] [OORB_MOOTA] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.^[2] [OORD_MOOTA] Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.^[3]

Publication Abstract from PubMed

Thiamine pyrophosphate (TPP), a derivative of vitamin B1, is a versatile and ubiquitous cofactor. When coupled with [4Fe-4S] clusters in microbial 2-oxoacid:ferredoxin oxidoreductases (OFORs), TPP is involved in catalyzing low-potential redox reactions that are important for the synthesis of key metabolites and the reduction of N2, H+, and CO2. We have determined the high-resolution (2.27 A) crystal structure of the TPP-dependent oxalate oxidoreductase (OOR), an enzyme that allows microbes to grow on oxalate, a widely occurring dicarboxylic acid that is found in soil and freshwater and is responsible for kidney stone disease in humans. OOR catalyzes the anaerobic oxidation of oxalate, harvesting the low-potential electrons for use in anaerobic reduction and fixation of CO2. We compare the OOR structure to that of the only other structurally characterized OFOR family member, pyruvate:ferredoxin oxidoreductase. This side-by-side structural analysis highlights the key similarities and differences that are relevant for the chemistry of this entire class of TPP-utilizing enzymes.

The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism.,Gibson MI, Brignole EJ, Pierce E, Can M, Ragsdale SW, Drennan CL Biochemistry. 2015 Jun 24. PMID:26061898^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pierce E, Becker DF, Ragsdale SW. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. J Biol Chem. 2010 Dec 24;285(52):40515-24. doi: 10.1074/jbc.M110.155739. Epub, 2010 Oct 18. PMID:20956531 doi:http://dx.doi.org/10.1074/jbc.M110.155739
↑ Pierce E, Becker DF, Ragsdale SW. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. J Biol Chem. 2010 Dec 24;285(52):40515-24. doi: 10.1074/jbc.M110.155739. Epub, 2010 Oct 18. PMID:20956531 doi:http://dx.doi.org/10.1074/jbc.M110.155739
↑ Pierce E, Becker DF, Ragsdale SW. Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate. J Biol Chem. 2010 Dec 24;285(52):40515-24. doi: 10.1074/jbc.M110.155739. Epub, 2010 Oct 18. PMID:20956531 doi:http://dx.doi.org/10.1074/jbc.M110.155739
↑ Gibson MI, Brignole EJ, Pierce E, Can M, Ragsdale SW, Drennan CL. The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 2015 Jun 24. PMID:26061898 doi:http://dx.doi.org/10.1021/acs.biochem.5b00521

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c4i"

@@ Line 6: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxalate_oxidoreductase Oxalate oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.7.10 1.2.7.10] </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=5c4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c4i OCA], [http://pdbe.org/5c4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c4i RCSB], [http://www.ebi.ac.uk/pdbsum/5c4i 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=5c4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c4i OCA], [http://pdbe.org/5c4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c4i RCSB], [http://www.ebi.ac.uk/pdbsum/5c4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c4i ProSAT]</span></td></tr>
 </table>
 == Function ==

5c4i

From Proteopedia

Revision as of 16:29, 15 November 2017

Structure of an Oxalate Oxidoreductase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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