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

被引:29
|
作者
Kudo, N
Allen, MD
Koike, H
Katsuya, Y
Suzuki, M
机构
[1] AIST NIBHT, CREST Ctr Struct Biol, Tsukuba, Ibaraki 3050046, Japan
[2] Univ Tokyo, Grad Sch Human & Environm Sci, Meguro Ku, Tokyo 1538902, Japan
[3] Hyogo Prefectural Inst Ind Res, Suma Ku, Kobe, Hyogo 6540037, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷
关键词
D O I
10.1107/S0907444900020369
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom using a conventional X-ray source and to 1.8 Angstrom 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 Angstrom. In combination with diffraction data obtained from K-2[Pt(CN)(6)] and K(AuCl4) derivatives, an electron-density map was calculated at a resolution of 3.0 Angstrom. Four monomers were identified in the asymmetric unit, with four beta -strands and two alpha -helices in each monomer.
引用
收藏
页码:469 / 471
页数:3
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