Ontology highlight
ABSTRACT:
SUBMITTER: Mhashal AR
PROVIDER: S-EPMC5572915 | biostudies-literature | 2017 Aug
REPOSITORIES: biostudies-literature
Mhashal Anil R AR Vardi-Kilshtain Alexandra A Kohen Amnon A Major Dan Thomas DT
The Journal of biological chemistry 20170615 34
A key question concerning the catalytic cycle of <i>Escherichia coli</i> dihydrofolate reductase (<i>ec</i>DHFR) is whether the Met<sup>20</sup> loop is dynamically coupled to the chemical step during catalysis. A more basic, yet unanswered question is whether the Met<sup>20</sup> loop adopts a closed conformation during the chemical hydride transfer step. To examine the most likely conformation of the Met<sup>20</sup> loop during the chemical step, we studied the hydride transfer in wild type ( ...[more]