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.
van den Bremer
Ewald T J
ET
Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research & Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands.
Keeble
Anthony H
AH
Kleanthous
Colin
C
Heck
Albert J R
AJ
D001665:Binding Sites; D002151:Calorimetry; D018360:Crystallography, X-Ray; D003851:Deoxyribonucleases / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D013058:Mass Spectrometry; D008670:Metals / Q000737:chemistry*; D015394:Molecular Structure; D010710:Phosphates / Q000737:chemistry*; D013329:Structure-Activity Relationship
D029968:Escherichia coli Proteins; D008670:Metals; D010710:Phosphates; D003851:Deoxyribonucleases