Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from Aeropyrum pernix and Sulfolobus tokodaii

被引：2

作者：

Shimizu, Satoru ^{[1
]}

Juan, Ella Czarina Magat ^{[1
]}

Miyashita, Yu-ichiro ^{[1
]}

Sato, Yoshiteru ^{[1
]}

Hoque, Md Mominul ^{[1
]}

Suzuki, Kaoru ^{[2
]}

Yogiashi, Masataka ^{[2
]}

Tsunoda, Masaru ^{[3
]}

Dock-Bregeon, Anne-Catherine ^{[4
]}

Moras, Dino ^{[4
]}

Sekiguchi, Takeshi ^{[2
]}

Takenaka, Akio ^{[1
,3
]}

机构：

[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Midori Ku, Yokohama, Kanagawa 2268501, Japan

[2] Iwaki Meisei Univ, Coll Sci & Engn, Fukushima 9708551, Japan

[3] Iwaki Meisei Univ, Fac Pharm, Fukushima 9708551, Japan

[4] Inst Genet & Biol Mol & Cellulaire, Dept Biol & Genom Struct, F-67404 Illkirch Graffenstaden, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

关键词：

D O I：

10.1107/S1744309108026924

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Threonyl-tRNA synthetase (ThrRS) plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr) and editing misacylation. ThrRS generally contains an N-terminal editing domain, a catalytic domain and an anticodon-binding domain. The sequences of the editing domain in ThrRSs from archaea differ from those in bacteria and eukaryotes. Furthermore, several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS. To reveal the structural basis for this evolutionary divergence, the two types of ThrRS from the crenarchaea A. pernix and S. tokodaii have been overexpressed in Eschericha coli, purified and crystallized by the hanging-drop vapour-diffusion method. Diffraction data were collected and the structure of a selenomethionine-labelled A. pernix type-1 ThrRS crystal has been solved using the MAD method.

引用

页码：903 / 910

页数：8

共 28 条

[11] HYDROLYTIC ACTION OF AMINOACYL-TRNA SYNTHETASES FROM BAKERS-YEAST - CHEMICAL PROOFREADING OF THR-T-RNA-VAL BY VALYL-T-RNA SYNTHETASE STUDIED WITH MODIFIED T-RNA-VAL AND AMINO-ACID ANALOGS [J].

IGLOI, GL ;

VONDERHAAR, F ;

CRAMER, F .

BIOCHEMISTRY, 1977, 16 (08) :1696-1702

[12] A freestanding proofreading domain is required for protein synthesis quality control in Archaea [J].

Korencic, D ;

Ahel, I ;

Schelert, J ;

Sacher, M ;

Ruan, BF ;

Stathopoulos, C ;

Blum, P ;

Ibba, M ;

Söll, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (28) :10260-10265

[13] SOLVENT CONTENT OF PROTEIN CRYSTALS [J].

MATTHEWS, BW .

JOURNAL OF MOLECULAR BIOLOGY, 1968, 33 (02) :491-+

[14] Phaser crystallographic software [J].

McCoy, Airlie J. ;

Grosse-Kunstleve, Ralf W. ;

Adams, Paul D. ;

Winn, Martyn D. ;

Storoni, Laurent C. ;

Read, Randy J. .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 2007, 40 :658-674

[15] AMORE - AN AUTOMATED PACKAGE FOR MOLECULAR REPLACEMENT [J].

NAVAZA, J .

ACTA CRYSTALLOGRAPHICA SECTION A, 1994, 50 :157-163

[16] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

[17] Automated protein model building combined with iterative structure refinement [J].

Perrakis, A ;

Morris, R ;

Lamzin, VS .

NATURE STRUCTURAL BIOLOGY, 1999, 6 (05) :458-463

[18] The structure of threonyl-tRNA synthetase-tRNAThr complex enlightens its repressor activity and reveals an essential zinc ion in the active site [J].

Sankaranarayanan, R ;

Dock-Bregeon, AC ;

Romby, P ;

Caillet, J ;

Springer, M ;

Rees, B ;

Ehresmann, C ;

Ehresmann, B ;

Moras, D .

CELL, 1999, 97 (03) :371-381

[19]

Sankaranarayanan R, 2000, NAT STRUCT BIOL, V7, P461

[20] Structure of the nondiscriminating aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7 reveals the recognition mechanism for two different tRNA anticodons [J].

Sato, Yoshiteru ;

Maeda, Yohei ;

Shimizu, Satoru ;

Hossain, Md Tofazzal ;

Ubukata, Souichirou ;

Suzuki, Kaoru ;

Sekiguchi, Takeshi ;

Takenaka, Akio .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2007, 63 :1042-1047

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