Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic archaeon.
A protein belonging to the Lrp/AsnC transcription-factor family, pot1216151, from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In Escherichia coli, leucine-responsive protein (Lrp) and AsnC regulate a number of metabolic genes. The crystals of pot1216151 diffracted to 2.3 A using a conventional X-ray source and to 1.8 A using a synchrotron-radiation source. The space group was identified to be P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.9, c = 98.5 A. In combination with diffraction data obtained from K(2)[Pt(CN)(6)] and K(AuCl(4)) derivatives, an electron-density map was calculated at a resolution of 3.0 A. Four monomers were identified in the asymmetric unit, with four beta-strands and two alpha-helices in each monomer.
AIST-NIBHT CREST Centre of Structural Biology, 1-1 Higashi, Tsukuba 305-0046, Japan.
N
N
Kudo
M D
MD
Allen
H
H
Koike
Y
Y
Katsuya
M
M
Suzuki
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins; D051756:Leucine-Responsive Regulatory Protein; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D019711:Pyrococcus / Q000737:chemistry*; D014157:Transcription Factors
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C497278:Lrp protein, E coli; D014157:Transcription Factors; D051756:Leucine-Responsive Regulatory Protein