Structure of the fMet-tRNAfMet-binding domain of B.stearothermophilus initiation factor IF2

被引：60

作者：

Meunier, S

Spurio, R

Czisch, M

Wechselberger, R

Guenneugues, M

Gualerzi, CO

Boelens, R

机构：

[1] Univ Utrecht, Bijvoet Ctr Biomol Res, NL-3584 CH Utrecht, Netherlands

[2] Univ Camerino, Dipartimento Biol MCA, Genet Lab, I-62032 Camerino, MC, Italy

来源：

EMBO JOURNAL | 2000年 / 19卷 / 08期

关键词：

bacterial translation; NMR; protein; protein biosynthesis; ribosome;

D O I：

10.1093/emboj/19.8.1918

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：

The three-dimensional structure of the fMet-tRNA(fMet) -binding domain of translation initiation factor IF2 from Bacillus stearothermophilus has been determined by heteronuclear NMR spectroscopy. Its structure consists of six antiparallel beta-strands, connected via loops, and forms a closed beta-barrel similar to domain II of elongation factors EF-Tu and EF-F, despite low sequence homology. Two structures of the ternary complexes of the EF-Tu.aminoacyl-tRNA. GDP analogue have been reported and were used to propose and discuss the possible fMet-tRNA(fMet)-binding site of IF2.

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页码：1918 / 1926

页数：9

相关论文

共 52 条

[1] An alpha to beta conformational switch in EF-Tu [J].

Abel, K ;

Yoder, MD ;

Hilgenfeld, R ;

Jurnak, F .

STRUCTURE, 1996, 4 (10) :1153-1159

[2] 3-DIMENSIONAL STRUCTURE OF THE RIBOSOMAL TRANSLOCASE - ELONGATION-FACTOR-G FROM THERMUS-THERMOPHILUS [J].

AEVARSSON, A ;

BRAZHNIKOV, E ;

GARBER, M ;

ZHELTONOSOVA, J ;

CHIRGADZE, Y ;

AL-KARADAGHI, S ;

SVENSSON, LA ;

LILJAS, A .

EMBO JOURNAL, 1994, 13 (16) :3669-3677

[3] The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange [J].

Al-Karadaghi, S ;

AEvarsson, A ;

Garber, M ;

Zheltonosova, J ;

Liljas, A .

STRUCTURE, 1996, 4 (05) :555-565

[4] AN ALTERNATIVE 3D-NMR TECHNIQUE FOR CORRELATING BACKBONE N-15 WITH SIDE-CHAIN H-BETA-RESONANCES IN LARGER PROTEINS [J].

ARCHER, SJ ;

IKURA, M ;

TORCHIA, DA ;

BAX, A .

JOURNAL OF MAGNETIC RESONANCE, 1991, 95 (03) :636-641

[5] CRYSTAL-STRUCTURE OF ACTIVE ELONGATION-FACTOR TU REVEALS MAJOR DOMAIN REARRANGEMENTS [J].

BERCHTOLD, H ;

RESHETNIKOVA, L ;

REISER, COA ;

SCHIRMER, NK ;

SPRINZL, M ;

HILGENFELD, R .

NATURE, 1993, 365 (6442) :126-132

[6] STRUCTURE DETERMINATION OF A TETRASACCHARIDE - TRANSIENT NUCLEAR OVERHAUSER EFFECTS IN THE ROTATING FRAME [J].

BOTHNERBY, AA ;

STEPHENS, RL ;

LEE, JM ;

WARREN, CD ;

JEANLOZ, RW .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1984, 106 (03) :811-813

[7]

BOURNE HR, 1991, NATURE, V349, P117, DOI 10.1038/349117a0

[8] Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors [J].

Brock, S ;

Szkaradkiewicz, K ;

Sprinzl, M .

MOLECULAR MICROBIOLOGY, 1998, 29 (02) :409-417

[9]

BRUNGER A, 1992, X PLOR V3 1 MANUAL

[10] THE CRYSTAL-STRUCTURE OF ELONGATION-FACTOR-G COMPLEXED WITH GDP, AT 2.7-ANGSTROM RESOLUTION [J].

CZWORKOWSKI, J ;

WANG, J ;

STEITZ, TA ;

MOORE, PB .

EMBO JOURNAL, 1994, 13 (16) :3661-3668

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