Crystal structure of LexA: a conformational switch for regulation of self-cleavage
Article Abstract:
Crystallographic analysis explains the structural and energetic aspects of LexA repressor cleavage reactions in vivo and in vitro, requiring RecA and high pH, respectively. Data indicate that RecA stabilizes the clevable conformation of LexA repressor.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
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High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
Article Abstract:
Structural analysis reveal that the large ribosomal subunit of Deinococcus radiodurans eubacterium is composed of intersubunit bridges in unbound subunits, which allow movements of the L1-stalk, facilitating the exit of tRNA.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
User Contributions:
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