Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family.

ABSTRACT: LysR-type transcriptional regulators comprise the largest family of homologous regulatory DNA-binding proteins in bacteria. A problematic challenge in the crystallization of LysR-type regulators stems from the insolubility and precipitation difficulties encountered with high concentrations of the full-length versions of these proteins. A general oligomerization scheme is proposed for this protein family based on the structures of the effector-binding domain of BenM in two different space groups, P4(3)22 and C222(1). These structures used the same oligomerization scheme of dimer-dimer interactions as another LysR-type regulator, CbnR, the full-length structure of which is available [Muraoka et al. (2003), J. Mol. Biol. 328, 555-566]. Evaluation of packing relationships and surface features

SUBMITTER: Ezezika OC 

PROVIDER: S-EPMC2334995 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature