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Crystal structure of the Lrp‐like transcriptional regulator from the archaeon Pyrococcus furiosus
Author(s) -
Leonard Philip M.,
Smits Sander H.J.,
Sedelnikova Svetlana E.,
Brinkman Arie B.,
de Vos Willem M.,
van der Oost John,
Rice David W.,
Rafferty John B.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.5.990
Subject(s) - pyrococcus furiosus , biology , regulator , genetics , archaea , computational biology , gene
The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus 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 Å 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 α/β character reminiscent of a number of RNA‐ and DNA‐binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel β‐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.