Ontology highlight
ABSTRACT:
SUBMITTER: Jin J
PROVIDER: S-EPMC4319933 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Jin Jin J Wu Ruijuan R Zhu Jia J Yang Shaoyuan S Lei Zhen Z Wang Nan N Singh Vinay K VK Zheng Jimin J Jia Zongchao Z
PloS one 20150206 2
YhdE, a Maf-like protein in Escherichia coli, exhibits nucleotide pyrophosphatase (PPase) activity, yet its cellular function remains unknown. Here, we characterized the PPase activity of YhdE on dTTP, UTP and TTP and determined two crystal structures of YhdE, revealing 'closed' and 'open' conformations of an adaptive active site. Our functional studies demonstrated that YhdE retards cell growth by prolonging the lag and log phases, particularly under stress conditions. Morphology studies showed ...[more]