Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii

被引：4

作者：

Fukunaga, R

Yokoyama, S ^{[1
]}

机构：

[1] Univ Tokyo, Dept Biophys & Biochem, Grad Sch Sci, Tokyo, Japan

[2] RIKEN, Genom Sci Ctr, Wako, Saitama, Japan

[3] RIKEN, Harima Inst, SPring 8, Wako, Saitama, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S0907444904020700

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The leucyl-tRNA synthetase (LeuRS) from the archaeon Pyrococcus horikoshii was overexpressed in a C-terminally truncated form in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43 Angstrom, alpha = beta = 90, gamma = 120degrees. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 Angstrom(3) Da(-1) and a solvent content of 60.7%. A data set diffracting to 2.2 Angstrom resolution was collected from a single crystal at 100 K. Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the SAD phasing method.

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页码：1916 / 1918

页数：3

相关论文

共 17 条

[1] RECOGNITION NUCLEOTIDES OF ESCHERICHIA-COLI TRANSFER RNA(LEU) AND ITS ELEMENTS FACILITATING DISCRIMINATION FROM TRANSFER RNA(SER) AND TRANSFER RNA(TYR) [J].

ASAHARA, H ;

HIMENO, H ;

TAMURA, K ;

HASEGAWA, T ;

WATANABE, K ;

SHIMIZU, M .

JOURNAL OF MOLECULAR BIOLOGY, 1993, 231 (02) :219-229

[2] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].

BAILEY, S .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763

[3] ROOT OF THE UNIVERSAL TREE OF LIFE BASED ON ANCIENT AMINOACYL-TRANSFER-RNA SYNTHETASE GENE DUPLICATIONS [J].

BROWN, JR ;

DOOLITTLE, WF .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (07) :2441-2445

[4] The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue [J].

Cusack, S ;

Yaremchuk, A ;

Tukalo, M .

EMBO JOURNAL, 2000, 19 (10) :2351-2361

[5] tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding [J].

Delagoutte, B ;

Moras, D ;

Cavarelli, J .

EMBO JOURNAL, 2000, 19 (21) :5599-5610

[6] Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNAVal and valyl-tRNA synthetase [J].

Fukai, S ;

Nureki, O ;

Sekine, S ;

Shimada, A ;

Tao, JS ;

Vassylyev, DG ;

Yokoyama, S .

CELL, 2000, 103 (05) :793-803

[7] Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine [J].

Fukunaga, R ;

Fukai, S ;

Ishitani, R ;

Nureki, O ;

Yokoyama, S .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (09) :8396-8402

[8] EDITING OF ERRORS IN SELECTION OF AMINO-ACIDS FOR PROTEIN-SYNTHESIS [J].

JAKUBOWSKI, H ;

GOLDMAN, E .

MICROBIOLOGICAL REVIEWS, 1992, 56 (03) :412-429

[9] Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion [J].

Kobayashi, T ;

Nureki, O ;

Ishitani, R ;

Yaremchuk, A ;

Tukalo, M ;

Cusack, S ;

Sakamoto, K ;

Yokoyama, S .

NATURE STRUCTURAL BIOLOGY, 2003, 10 (06) :425-432

[10] Aminoacylation error correction [J].

Lin, L ;

Hale, SP ;

Schimmel, P .

NATURE, 1996, 384 (6604) :33-34