Towards a new T-fold protein?: the coproporphyrinogen III oxidase sequence matches many structural features from urate oxidase.
Urate oxidase (UOX) and coproporphyrinogen III oxidase (CPO) are two unusual oxidases as they accomplish their catalytic act with no co-factor nor metal ion. They both require molecular oxygen, and lead to hydrogen peroxide in addition to the product. UOX is composed of two contiguous Tunneling-fold domains and CPO appears to be also divided into two structurally equivalent domains. Moreover, each of these putative domains can be coherently aligned on UOX domains. Although their sequences are very distant, we therefore suggest that functional CPO dimer is built around a tunnel, with the substrate sitting above it, on the N- and C-terminal side. This overall model is supported by mutation data and is coherent with the chemical events expected for substrate processing by CPO.
Université de Caen, CNRS UMR6551, bd. Henri Becquerel, BP5229, 14074 Caen Cedex, France. n.colloch@neuro.unicaen.fr
Nathalie
N
Colloc'h
Jean-Paul
JP
Mornon
Jean-Michael
JM
Camadro
D000595:Amino Acid Sequence; D000818:Animals; D003304:Coproporphyrinogen Oxidase / Q000737:chemistry* / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010843:Pichia / Q000201:enzymology; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000201:enzymology; D013552:Swine; D014503:Urate Oxidase / Q000737:chemistry
D003304:Coproporphyrinogen Oxidase; D014503:Urate Oxidase