5C4I: Structure Of An Oxalate Oxidoreductase

Citation:
Abstract
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.
PDB ID: 5C4IDownload
MMDB ID: 130639
PDB Deposition Date: 2015/6/18
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.27  Å
Source Organism:
Similar Structures:
Biological Unit for 5C4I: hexameric; determined by author and by software (PISA)
Molecular Components in 5C4I
Label Count Molecule
Proteins (6 molecules)
2
Oxalate Oxidoreductase Subunit Alpha(Gene symbol: Moth_1592)
Molecule annotation
2
Oxalate Oxidoreductase Subunit Delta(Gene symbol: Moth_1593)
Molecule annotation
2
Oxalate Oxidoreductase Subunit Beta(Gene symbol: Moth_1591)
Molecule annotation
Chemicals (12 molecules)
1
6
2
2
3
2
4
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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