Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein RstDEAD from Bacillus stearothermophilus

被引:1
作者
Carmel, AB
Matthews, BW
机构
[1] Univ Oregon, Howard Hughes Med Inst, Inst Mol Biol, Eugene, OR 97403 USA
[2] Univ Oregon, Dept Chem, Eugene, OR 97403 USA
[3] Univ Oregon, Dept Phys, Eugene, OR 97403 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444903018389
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
DEAD proteins are members of a large and diverse family of RNA helicases that use energy from ATP hydrolysis to unwind short regions of duplex RNA. BstDEAD from Bacillus stearothermophilus is a 436-amino-acid protein and a representative member of the DEAD protein family. In addition to the mechanistic core common to DEAD proteins, BstDEAD has a unique similar to60-amino-acid C-terminal extension that may denote a specific biological role. BstDEAD has been crystallized in space group P4(1)/32(1)2, with unit-cell parameters a = b = 100.3, c = 110.6 Angstrom and one molecule per asymmetric unit. It is the first DEAD protein to be crystallized containing a unique extension outside of the core.
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页码:1869 / 1870
页数:2
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