Abstract
The crystal structure analysis of the complex RNase T1 • 2’-guanylic acid has provided insight into specific protein-nucleic acid interaction and into the mechanism of RNA hydrolysis catalyzed by RNase T1. Recognition of guanine is via hydrogen bonding of main chain dipeptide Asn43-Asn44 to O6 and N1-H of the base and additional stacking of Tyr45 with the guanine heterocycle and of Tyr42 with guanine O6. RNA hydrolysis is initiated by removal of a proton from O2, H by G1u58 followed by formation of a cyclic 2’,3’-guanylic acid, assisted by Arg77 and by His92. In a second step the cyclic intermediate is hydrolized by water to yield an RNA fragment with terminal 3’-guanylic acid.
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 callDisclaimer: 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.
