PMID:10873443
| Citation |
Grishin, NV (2000) C-terminal domains of Escherichia coli topoisomerase I belong to the zinc-ribbon superfamily. J. Mol. Biol. 299:1165-77 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1006/jmbi.2000.3841 |
| Keywords |
Amino Acid Sequence; Binding Sites; Cysteine/metabolism; DNA Topoisomerases, Type I/chemistry; DNA Topoisomerases, Type I/classification; DNA Topoisomerases, Type I/metabolism; Escherichia coli/enzymology; Evolution, Molecular; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/classification; Peptide Fragments/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factors/chemistry; Transcription Factors/metabolism; Zinc/metabolism |
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