Crystal Structure of Full Length Topoisomerase I from Thermotoga maritima
| Autor: | Bernd Wieland, Axel Harrenga, Dietmar Schomburg, Guido Hansen, Peter Reinemer |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
DNA
Bacterial Models Molecular Protein Conformation Stereochemistry Amino Acid Motifs Molecular Sequence Data Static Electricity Isomerase Crystallography X-Ray chemistry.chemical_compound Structural Biology Catalytic Domain Escherichia coli Humans Thermotoga maritima Topoisomerase III Amino Acid Sequence Molecular Biology Conserved Sequence Base Sequence Sequence Homology Amino Acid biology Topoisomerase biology.organism_classification Protein Structure Tertiary DNA Topoisomerases Type I Biochemistry chemistry Phosphodiester bond biology.protein DNA supercoil DNA Cysteine |
| Zdroj: | Journal of Molecular Biology. 358:1328-1340 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2006.03.012 |
| Popis: | DNA topoisomerases are a family of enzymes altering the topology of DNA by concerted breakage and rejoining of the phosphodiester backbone of DNA. Bacterial and archeal type IA topoisomerases, including topoisomerase I, topoisomerase III, and reverse gyrase, are crucial in regulation of DNA supercoiling and maintenance of genetic stability. The crystal structure of full length topoisomerase I from Thermotoga maritima was determined at 1.7 A resolution and represents an intact and fully active bacterial topoisomerase I. It reveals the torus-like structure of the conserved transesterification core domain comprising domains I–IV and a tightly associated C-terminal zinc ribbon domain (domain V) packing against domain IV of the core domain. The previously established zinc-independence of the functional activity of T. maritima topoisomerase I is further supported by its crystal structure as no zinc ion is bound to domain V. However, the structural integrity is preserved by the formation of two disulfide bridges between the four Zn-binding cysteine residues. A functional role of domain V in DNA binding and recognition is suggested and discussed in the light of the structure and previous biochemical findings. In addition, implications for bacterial topoisomerases I are provided. |
| Databáze: | OpenAIRE |
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