1I1G

CRYSTAL STRUCTURE OF THE LRP-LIKE TRANSCRIPTIONAL REGULATOR FROM THE ARCHAEON PYROCOCCUS FURIOSUS

Summary for 1I1G

• Entry DOI: 10.2210/pdb1i1g/pdb
• Descriptor: TRANSCRIPTIONAL REGULATOR LRPA (1 entity in total)
• Functional Keywords: helix-turn-helix, lrp/asnc family, pyrococcus furiosus, transcriptional regulator, transcription
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 31835.58

Authors

Leonard, P.M.,Smits, S.H.J.,Sedelnikova, S.E.,Brinkman, A.B.,de Vos, W.M.,van der Oost, J.,Rice, D.W.,Rafferty, J.B. (deposition date: 2001-02-01, release date: 2002-02-06, Last modification date: 2024-02-07)

Primary citation

Leonard, P.M.,Smits, S.H.,Sedelnikova, S.E.,Brinkman, A.B.,de Vos, W.M.,van der Oost, J.,Rice, D.W.,Rafferty, J.B.
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus.
EMBO J., 20:990-997, 2001

PubMed Abstract: 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.

PubMed: 11230123
DOI: 10.1093/emboj/20.5.990

Experimental method

X-RAY DIFFRACTION (2.9 Å)