1i1g
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CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS
OverviewOverview
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 A 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.
About this StructureAbout this Structure
1I1G is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus., Leonard PM, Smits SH, Sedelnikova SE, Brinkman AB, de Vos WM, van der Oost J, Rice DW, Rafferty JB, EMBO J. 2001 Mar 1;20(5):990-7. PMID:11230123
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