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- W2000647640 abstract "Detection of remote evolutionary connections is increasingly difficult with sequence and structural divergence. A combination of sequence and structural analysis, in which statistically supported sequence similarity had a crucial impact, revealed that Escherichia coli topoisomerase I C-terminal fragment is evolutionarily related to the three tetracysteine zinc-binding domains of the enzyme. Spatial structure analysis of this C-terminal fragment indicates that it consists of two structurally similar domains and suggests homology between them. Sequence similarity between the zinc-binding domains of type Ia topoisomerases and transcription regulators of known spatial structure helps to conclude that E. coli topo I contains five copies of a zinc ribbon domain at the C terminus. Two of these domains, corresponding to the C-terminal fragment, lost their cysteine residues and are probably not able to bind zinc. Present analyses lead to the classification of the C-terminal fragment of E. coli topoisomerase I as a member of zinc ribbon superfamily, despite the absence of zinc-binding sites." @default.
- W2000647640 created "2016-06-24" @default.
- W2000647640 creator A5039591575 @default.
- W2000647640 date "2000-06-01" @default.
- W2000647640 modified "2023-09-25" @default.
- W2000647640 title "C-terminal domains of Escherichia coli topoisomerase I belong to the zinc-ribbon superfamily" @default.
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- W2000647640 doi "https://doi.org/10.1006/jmbi.2000.3841" @default.
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