Three-dimensional structure of Escherichia coli RNA polymerase holoenzyme determined by electron crystallography

Nature ◽  
1989 ◽  
Vol 340 (6236) ◽  
pp. 730-732 ◽  
Author(s):  
Seth A. Darst ◽  
Elizabeth W. Kubalek ◽  
Roger D. Kornberg
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Electron Crystallography ◽  
Three Dimensional Structure ◽  
Rna Polymerase Holoenzyme

Sequence-specific1H n.m.r. assignments and determination of the three-dimensional structure of reduced escherichia coli glutaredoxin

1991 ◽  
Vol 221 (4) ◽  
pp. 1311-1324 ◽  
Author(s):  
Patrick Sodano ◽  
Tai-he Xia ◽  
John H. Bushweller ◽  
Olof Björnberg ◽  
Arne Holmgren ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Three-Dimensional Structure of Escherichia coli Dihydrodipicolinate Reductase

Biochemistry ◽  
1995 ◽  
Vol 34 (11) ◽  
pp. 3502-3512 ◽  
Author(s):  
Giovanna Scapin ◽  
John S. Blanchard ◽  
James C. Sacchettini
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

scholarly journals RNA minihelices as model substrates for ATP/CTP:tRNA nucleotidyltransferase

1997 ◽  
Vol 327 (3) ◽  
pp. 847-851 ◽  
Author(s):  
Zengji LI ◽  
Yue SUN ◽  
L. David THURLOW
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Single Base ◽  
Three Dimensional Structure ◽  
E Coli ◽  
Base Identity

Twenty-one RNA minihelices, resembling the coaxially stacked acceptor- /T-stems and T-loop found along the top of a tRNA's three-dimensional structure, were synthesized and used as substrates for ATP/CTP:tRNA nucleotidyltransferases from Escherichia coli and Saccharomyces cerevisiae. The sequence of nucleotides in the loop varied at positions corresponding to residues 56, 57 and 58 in the T-loop of a tRNA. All minihelices were substrates for both enzymes, and the identity of bases in the loop affected the interaction. In general, RNAs with purines in the loop were better substrates than those with pyrimidines, although no single base identity absolutely determined the effectiveness of the RNA as substrate. RNAs lacking bases near the 5ʹ-end were good substrates for the E. coli enzyme, but were poor substrates for that from yeast. The apparent Km values for selected minihelices were 2-3 times that for natural tRNA, and values for apparent Vmax were lowered 5-10-fold.

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