The TIM-barrel fold: a versatile framework for efficient enzymes.
Recent studies on triosephosphate isomerase (TIM)-barrel enzymes highlight the remarkable versatility of the TIM-barrel scaffold. At least 15 distinct enzyme families use this framework to generate the appropriate active site geometry, always at the C-terminal end of the eight parallel beta-strands of the barrel. Sequence and structure comparisons now suggest that many of the TIM-barrel enzymes are evolutionarily related. Common structural properties of TIM-barrel enzymes are discussed.
Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, Oulu, Finland. rik.wierenga@oulu.fi
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D001665:Binding Sites; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D019143:Evolution, Molecular; D008958:Models, Molecular; D011487:Protein Conformation; D014305:Triose-Phosphate Isomerase / Q000737:chemistry* / Q000378:metabolism
D014305:Triose-Phosphate Isomerase