Functional convergence of two lysyl-tRNA synthetases with unrelated topologies

被引：64

作者：

Terada, T

Nureki, O

Ishitani, R

Ambrogelly, A

Ibba, M

Söll, D

Yokoyama, S

机构：

[1] RIKEN, Genom Sci Ctr, Yokohama, Kanagawa 2300045, Japan

[2] RIKEN, Harima Inst Spring8, Sayo, Hyogo 6795148, Japan

[3] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Tokyo 113, Japan

[4] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[5] Ohio State Univ, Dept Microbiol, Columbus, OH 43210 USA

[6] Yale Univ, Dept Chem, New Haven, CT 06520 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 04期

关键词：

D O I：

10.1038/nsb777

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Lysyl-tRNA can be synthesized by both a class I (LysRS-I) and a class II (LysRS-II) lysyl-tRNA synthetase. The crystal structure of LysRS-I from Pyrococcus horikoshii at 2.6 Angstrom resolution reveals extensive similarity with glutamyl-tRNA synthetase (GluRS). A comparison of the structures of LysRS-I and LysRS-II in complex with lysine shows that both enzymes use similar strategies for substrate recognition within unrelated active site topologies. A docking model based upon the GluRS-tRNA complex suggests how LysRS-I and LysRS-II can recognize the same molecular determinants in tRNA(Lys), as shown by biochemical results, while approaching the acceptor helix of the tRNA from opposite sides.

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页码：257 / 262

页数：6

相关论文

共 34 条

[1] Methods used in the structure determination of bovine mitochondrial F-1 ATPase [J].

Abrahams, JP ;

Leslie, AGW .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :30-42

[2] Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement [J].

Adams, PD ;

Pannu, NS ;

Read, RJ ;

Brunger, AT .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (10) :5018-5023

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

BAILEY, S .

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

[4] Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii [J].

Bult, CJ ;

White, O ;

Olsen, GJ ;

Zhou, LX ;

Fleischmann, RD ;

Sutton, GG ;

Blake, JA ;

FitzGerald, LM ;

Clayton, RA ;

Gocayne, JD ;

Kerlavage, AR ;

Dougherty, BA ;

Tomb, JF ;

Adams, MD ;

Reich, CI ;

Overbeek, R ;

Kirkness, EF ;

Weinstock, KG ;

Merrick, JM ;

Glodek, A ;

Scott, JL ;

Geoghagen, NSM ;

Weidman, JF ;

Fuhrmann, JL ;

Nguyen, D ;

Utterback, TR ;

Kelley, JM ;

Peterson, JD ;

Sadow, PW ;

Hanna, MC ;

Cotton, MD ;

Roberts, KM ;

Hurst, MA ;

Kaine, BP ;

Borodovsky, M ;

Klenk, HP ;

Fraser, CM ;

Smith, HO ;

Woese, CR ;

Venter, JC .

SCIENCE, 1996, 273 (5278) :1058-1073

[5] Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase [J].

Chihade, JW ;

Brown, JR ;

Schimmel, PR ;

de Pouplana, LR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (22) :12153-12157

[6] tRNA anticodon recognition and specification within subclass IIb aminoacyl-tRNA synthetases [J].

Commans, S ;

Lazard, M ;

Delort, F ;

Blanquet, S ;

Plateau, P .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 278 (04) :801-813

[7] 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

[8] 11 DOWN AND 9 TO GO [J].

CUSACK, S .

NATURE STRUCTURAL BIOLOGY, 1995, 2 (10) :824-831

[9] The crystal structures of T-thermophilus lysyl-tRNA synthetase complexed with E-coli tRNA(Lys) and a T-thermophilus tRNA(Lys) transcript: Anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue [J].

Cusack, S ;

Yaremchuk, A ;

Tukalo, M .

EMBO JOURNAL, 1996, 15 (22) :6321-6334

[10] Aminoacyl-tRNA synthetases: potential markers of genetic code development [J].

de Pouplana, LR ;

Schimmel, P .

TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (10) :591-596

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