Strategies for crystallization of protein/DNA bound complex by in situ phosphorylation of aspartic residue using 5'-phosphorylated-DNA.
We explore an opportunities that lie at the interface of chemistry and biology to generate the processes with novel biological and chemical properties. Our goal is to create complex of DNA molecules in series of operation directed toward efficient protein phosphorylation beyond autophosphorylating kinases for protein/DNA complex formation. The NarL protein is a model of our studies. From crystal structure of NarL and one of its domain-NarLC/DNA complex it is suggested that upon phosphorylation of Asp(59), NarL must open compacted pair of domains, the NarLN and NarLC to receive DNA molecule in the pathway that is yet not elucidated. We try to understand such process using programmed 5'-phosphorylated DNA for simultaneous NarL protein phosphorylation and DNA binding.
Grzeskowiak
Kazimierz
K
University of California Los Angeles, Los Angeles, CA 90095-1570, USA.
D001224:Aspartic Acid / Q000737:chemistry / Q000378:metabolism*; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010766:Phosphorylation
D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C069780:NarL protein, E coli; D001224:Aspartic Acid; D004247:DNA