Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 41, Issue -, Pages 54-61Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2016.05.011
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Funding
- National Institutes of Health [GM069857]
- National Science Foundation (NSF) Graduate Research Fellowship [1122374]
- Martin Family Society of Fellows for Sustainability
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2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon carbon bonds, generating low potential (similar to-500 mV) electrons. Crystallographic analysis of a recently discovered OFOR, an oxalate oxidoreductase (OOR), has provided a second view of OFOR architecture and active site composition. Using these recent structural data along with the previously determined structures of pyruvate:ferredoxin oxidoreductase, structure function relationships in this superfamily have been expanded and re-evaluated. Additionally, structural motifs have been defined that better serve to distinguish one OFOR subfamily from another and potentially uncover novel OFORs.
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