3-DIMENSIONAL MODELS OF THE GDP AND GTP FORMS OF THE GUANINE-NUCLEOTIDE DOMAIN OF ESCHERICHIA-COLI ELONGATION FACTOR-TU

被引：33

作者：

JURNAK, F

HEFFRON, S

SCHICK, B

DELARIA, K

机构：

[1] Department of Biochemistry, University of California, Riverside, CA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1050卷 / 1-3期

关键词：

Elongation factor Tu; Guanine nucleotide binding; ras p21;

D O I：

10.1016/0167-4781(90)90168-2

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：

Three-dimensional models of the GDP and GTP forms of the guanine nucleotide domain of Escherichia coli elongation factor Tu have been derived from the atomic coordinates of the trypsin-modified form of EF-Tu-GDP and by comparison with the ras p21 structures. The significance of the differences in the guanine nucleotide binding sites of EF-Tu and ras p21 are discussed. Crystallization of the EF-Tu-GMPPNP complex is reported. © 1990.

引用

页码：209 / 214

页数：6

共 14 条

[1]

BOURNE HR, 1990, UNPUB NATURE

[2] PREPARATION OF ESCHERICHIA-COLI ELONGATION-FACTOR TU-GUANOSINE 5'-TRIPHOSPHATE ANALOGS [J].