Understanding the nuclease activity of Xanthomonas albilineans Cas2 via its solution structure and dynamics

Cas2;nuclease activity;structure and dynamics;NMR;630

농업생명과학대학 농생명공학부 ;

University:서울대학교 대학원

关键词: Cas2;    nuclease activity;    structure and dynamics;    NMR;    630;   

Others  :  http://s-space.snu.ac.kr/bitstream/10371/141775/1/000000149673.pdf

美国|英语

来源: Seoul National University Open Repository

【 摘 要 】

and, the NMR relaxation data indicates that the active site and hinge regions possess highly dynamical motion as for the driving force of conformational change. In conclusion, the results suggest that XaCas2 is thermodynamically stable as inactive conformation in solution, and the forces from highly dynamic regions allow catalytically active conformation when encounter genetic substrates and preferred metal ions. Taken together, the intrinsic function of Cas2 can be explained by a dynamic equilibrium of conformational states that serves as a scaffold and as a nuclease on demand.