scholarly journals Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli.

1987 ◽  
Vol 84 (16) ◽  
pp. 5690-5694 ◽  
Author(s):  
J. P. Priestle ◽  
M. G. Grutter ◽  
J. L. White ◽  
M. G. Vincent ◽  
M. Kania ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Bifunctional Enzyme ◽  
Glycerol Phosphate ◽  
Three Dimensional Structure ◽  
Phosphate Synthase

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.

scholarly journals Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals

2008 ◽  
Vol 161 (3) ◽  
pp. 411-418 ◽  
Author(s):  
Guo-Bin Hu ◽  
William J. Rice ◽  
Stefan Dröse ◽  
Karlheinz Altendorf ◽  
David L. Stokes
Keyword(s):  
Escherichia Coli ◽  
Electron Tomography ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Three Dimensional Structure

scholarly journals FpvA-Mediated Ferric Pyoverdine Uptake in Pseudomonas aeruginosa: Identification of Aromatic Residues in FpvA Implicated in Ferric Pyoverdine Binding and Transport

2005 ◽  
Vol 187 (24) ◽  
pp. 8511-8515 ◽  
Author(s):  
Jiang-Sheng Shen ◽  
Valérie Geoffroy ◽  
Shadi Neshat ◽  
Zongchao Jia ◽  
Allison Meldrum ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Dimensional Structure ◽  
Aromatic Residues ◽  
Three Dimensional Structure

ABSTRACT A number of aromatic residues were seen to cluster in the upper portion of the three-dimensional structure of the FpvA ferric pyoverdine receptor of Pseudomonas aeruginosa, reminiscent of the aromatic binding pocket for ferrichrome in the FhuA receptor of Escherichia coli. Alanine substitutions in three of these, W362, W391, and F795, markedly compromised ferric pyoverdine binding and transport, consistent with a role of FpvA in ferric pyoverdine recognition.

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