The role of monovalent cations in the ATPase reaction of DNA gyrase

Four new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase have been determined. One of these, solved in the presence of K(+), is the highest resolution structure reported so far for this domain and, in conjunction with the three other structures, reveals new...

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Detalles Bibliográficos
Autores principales: Hearnshaw, Stephen James, Chung, Terence Tsz-Hong, Stevenson, Clare Elizabeth Mary, Maxwell, Anthony, Lawson, David Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2015
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388272/
https://www.ncbi.nlm.nih.gov/pubmed/25849408
http://dx.doi.org/10.1107/S1399004715002916

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4388272/
https://www.ncbi.nlm.nih.gov/pubmed/25849408
http://dx.doi.org/10.1107/S1399004715002916

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