Journal
EMBO JOURNAL
Volume 20, Issue 5, Pages 990-997Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.5.990
Keywords
helix-turn-helix; Lrp-AsnC family; Pyrococcus furiosus; transcriptional regulator; X-ray crystallography
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Funding
- Wellcome Trust Funding Source: Medline
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The LrpA protein from the hyperthermophilic archaeon Pyrococcusfuriosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 Angstrom resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta -sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.
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