Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic archaeon

Citation
N. Kudo et al., Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic archaeon, ACT CRYST D, 57, 2001, pp. 469-471
Citations number
16
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
0907-4449 → ACNP
Volume
57
Year of publication
2001
Part
3
Pages
469 - 471
Database
ISI
SICI code
0907-4449(200103)57:<469:CASDOA>2.0.ZU;2-V
Abstract
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 n umber of metabolic genes. The crystals of pot1216151 diffracted to 2.3 Angs trom using a conventional X-ray source and to 1.8 Angstrom using a synchrot ron-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 Angstrom. In combinati on with diffraction data obtained from K-2[Pt(CN)(6)] and K(AuCl4) derivati ves, an electron-density map was calculated at a resolution of 3.0 Angstrom . Four monomers were identified in the asymmetric unit, with four beta -str ands and two alpha -helices in each monomer.