Article
Impacts of mutations on dynamic allostery of adenylate kinase.
The Journal of chemical physics - 21 Jul 2021
Song Haoyu, Wutthinitikornkit Yanee, Zhou Xiaozhou, Li Jingyuan
Abstract excerpt
Escherichia coli adenylate kinase (AK) is composed of CORE domain and two branch domains: LID and AMP-binding domain (AMPbd). AK exhibits considerable allostery in a reversible phosphoryl transfer reaction, which is largely attributed to the relative motion of LID and AMPbd with respect to CORE. Such an allosteric conformational change is also evident in the absence of ligands. Recent studies showed that the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
