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The structure of AbrB, a transition state regulator in Bacillus subtilis, reveals a novel mode of DNA recognition and suggests that the protein is able to structurally conform to target DNA, both in terms of its multimeric state and in the positioning of its unique DNA binding domain.
The electron and X-ray crystallographic structures of AQP1 and GlpF, respectively, provide insights into the mechanisms of how water and small solutes such as glycerol selectively traverse lipid bilayers.
The structure of the Rad53p FHA domain reveals a new fundamental mechanism governing phosphothreonine-dependent protein–protein interactions in nuclear processes including DNA repair and replication in a broad range of organisms.
Many biological processes require the ordered assembly and disassembly of complex structures. By using common structural elements, conformational switching and competitive interactions, the proper temporal assembly of the structures is assured, while simultaneously taking full advantage of combinatorial flexibility.