2ivh
|
CRYSTAL STRUCTURE OF THE NUCLEASE DOMAIN OF COLE7 (H545Q MUTANT) IN COMPLEX WITH AN 18-BP DUPLEX DNA
OverviewOverview
Nonspecific endonucleases hydrolyze DNA without sequence specificity but, with sequence preference, however the structural basis for cleavage, preference remains elusive. We show here that the nonspecific endonuclease, ColE7 cleaves DNA with a preference for making nicks after (at 3'O-side), thymine bases but the periplasmic nuclease Vvn cleaves DNA more evenly, with little sequence preference. The crystal structure of the 'preferred, complex' of the nuclease domain of ColE7 bound to an 18 bp DNA with a, thymine before the scissile phosphate had a more distorted DNA phosphate, backbone than the backbones in the non-preferred complexes, so that the, scissile phosphate was compositionally closer to the endonuclease active, site resulting in more efficient DNA cleavage. On the other hand, in ... [(full description)]
About this StructureAbout this Structure
2IVH is a [Protein complex] structure of sequences from [Escherichia coli] with ZN as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for sequence-dependent DNA cleavage by nonspecific endonucleases., Wang YT, Yang WJ, Li CL, Doudeva LG, Yuan HS, Nucleic Acids Res. 2007;35(2):584-94. Epub 2006 Dec 15. PMID:17175542
Page seeded by OCA on Mon Oct 29 18:53:15 2007