Preliminary characterization by X-ray diffraction and Raman spectroscopy of a crystalline complex of Bacillus stearothermophilus initiation factor 2 C-domain and fMet-tRNAfMet

被引：10

作者：

Förster, C

Krafft, C

Welfle, H

Gualerzi, CO

Heinemann, U

机构：

[1] Max Delbruck Ctr Mol Med, Forsch Grp Kristallog, D-13122 Berlin, Germany

[2] Max Delbruck Ctr Mol Med, Forsch Grp Biopolymerspektroskopie, D-13122 Berlin, Germany

[3] Univ Camerino, Dept Cell Biol, Genet Lab, I-62032 Camerino, Italy

[4] Free Univ Berlin, Inst Kristallog, D-14195 Berlin, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444998014577

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Bacillus stearothermophilus translation initiation factor 2 (IF2) specifically binds initiator fMet-tRNA(fMet) and positions it into the ribosomal peptidyl site in the course of the initiation of protein biosynthesis. The isolated C-terminal domain of IF2 is capable of binding PMet-tRNA(fMet). as shown by RNase A and hydrolysis protection experiments. In the presence of fMet-tRNA(fMet), the IF2 C-domain yielded orthorhombic crystals of space group I222 (I2(1)2(1)2(1)) diffracting to 3.4 Angstrom resolution. The existence of equimolar amounts of tRNA and protein in the crystals was proven bq Raman spectroscopy. The observed unit cell suggests the presence of two IF2 C-domain-fMet-tRNA(fMet) complexes per asymmetric unit of the crystal.

引用

页码：712 / 716

页数：5

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