Abstract
24 European Crystallographic Meeting, ECM24, Marrakech, 2007 Page s129 Acta Cryst. (2007). A63, s129 motif, while the C-terminal domain shows a typical restriction endonuclease fold. By structural comparison and mutational analysis we showed that the active site of SdaI is located at the C-terminal domain and exhibits a new variation of the canonical PD...(D/E)XK active site motif. Mutational analysis of the residues from the predicted recognition helix of the wHTH motif suggests that SdaI determinants of sequence specificity are clustered at the N-terminal domain. The modular architecture of SdaI, wherein one domain mediates DNA binding while the other domain is predicted to catalyze hydrolysis, distinguishes SdaI from the previously characterized restriction enzymes interacting with symmetric recognition sequences.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Acta Crystallographica Section A Foundations of Crystallography
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
