Structural basis for interaction between mycobacterium smegmatis Ms6564, a TetR family master regulator, and its target DNA

Abstract

Background: The structural basis for interaction between a master regulator and DNA remains unclear. Results: We solved the crystal structures of a broad regulator Ms6564 and its protein-operator complex. Conclusion: Ms6564 binds DNA with strong affinity but makes flexible contacts with DNA. Significance: Ms6564 might slide more easily along the genomic DNA and extensively regulate the expression of diverse genes. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.