Metal induced selectivity in phosphate ion binding in E9 DNase.
Mass spectrometric and calorimetric data reveal that phosphate ion binding to the active site of colicin E9 DNase is delicately regulated by concomitant binding of specific transition metal ions.
Principais autores: | van den Bremer, E, Keeble, A, Kleanthous, K, Heck, A |
---|---|
Formato: | Journal article |
Idioma: | English |
Publicado em: |
2005
|
Registros relacionados
-
Calorimetric dissection of colicin DNase--immunity protein complex specificity.
por: Keeble, A, et al.
Publicado em: (2006) -
Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9.
por: Keeble, A, et al.
Publicado em: (2002) -
Ligand-induced changes in the conformational dynamics of a bacterial cytotoxic endonuclease.
por: van den Bremer, E, et al.
Publicado em: (2004) -
DNase I Footprinting to Identify Protein Binding Sites
por: Isabelle Gaugué, et al.
Publicado em: (2013-07-01) -
Structure of the ultra-high-affinity colicin E2 DNase--Im2 complex.
por: Wojdyla, J, et al.
Publicado em: (2012)