5C4I
Structure of an Oxalate Oxidoreductase
Summary for 5C4I
| Entry DOI | 10.2210/pdb5c4i/pdb |
| Descriptor | Oxalate oxidoreductase subunit alpha, Oxalate oxidoreductase subunit delta, Oxalate oxidoreductase subunit beta, ... (8 entities in total) |
| Functional Keywords | oxalate, oxidoreductase, ofor, thiamine |
| Biological source | Moorella thermoacetica (strain ATCC 39073) More |
| Total number of polymer chains | 6 |
| Total formula weight | 227006.92 |
| Authors | Gibson, M.I.,Brignole, E.J.,Pierce, E.,Can, M.,Ragsdale, S.W.,Drennan, C.L. (deposition date: 2015-06-18, release date: 2015-07-01, Last modification date: 2024-03-06) |
| Primary citation | Gibson, M.I.,Brignole, E.J.,Pierce, E.,Can, M.,Ragsdale, S.W.,Drennan, C.L. The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry, 54:4112-4120, 2015 Cited by PubMed 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 Å) 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. PubMed: 26061898DOI: 10.1021/acs.biochem.5b00521 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.274 Å) |
Structure validation
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