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.

Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model

2013 ◽  
Vol 798-799 ◽  
pp. 1095-1098
Author(s):  
Shi Ping Shan ◽  
Dong Xia Du ◽  
De Yuan Zhang ◽  
Zhao Hui Guo
Keyword(s):  
Brush Border Membrane ◽  
Molecular Model ◽  
Membrane Vesicle ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Dimensional Structure ◽  
Substrate Binding Pocket ◽  
Functional Interpretation ◽  
Three Dimensional Structure

Activated toxins interact with α-amylase receptor on the brush border membrane vesicle (BBMV) of the midgut epithelium, which activates intracellular oncotic pathways and leads to cell death. In order to decipher the mechanism of process how toxins interact with their receptors, it is essential to investigate their three-dimensional structure. The three-dimensional structure of α-amylase was constructed by homology modeling, based on crystal structure ofBacillus cereusoligo-1,6-glucosidase and the model was further evaluated using PROSA energy and ERRAT. The substrate binding pocket responsible for the interactions with toxins was predicted and analyzed, and the important role of binding of toxin to binding pocket on α-amylase was discussed in the aspect of Cry4Ba and Cry11Aa toxicity.

scholarly journals Nondiffusive Transport in Tokamaks: Three-Dimensional Structure of Bursts and the Role of Zonal Flows

2000 ◽  
Vol 85 (23) ◽  
pp. 4892-4895 ◽  
Author(s):  
P. Beyer ◽  
S. Benkadda ◽  
X. Garbet ◽  
P. H. Diamond
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Zonal Flows ◽  
Three Dimensional Structure

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

A detailed model of the three-dimensional structure of Escherichia coli 16 S ribosomal RNA in situ in the 30 S subunit

1988 ◽  
Vol 199 (1) ◽  
pp. 115-136 ◽  
Author(s):  
Richard Brimacombe ◽  
Johannes Atmadja ◽  
Wolfgang Stiege ◽  
Dierk Schüler
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Detailed Model ◽  
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 Escherichia coli thioredoxin-S2 to 2.8 A resolution.

1975 ◽  
Vol 72 (6) ◽  
pp. 2305-2309 ◽  
Author(s):  
A. Holmgren ◽  
B. O. Soderberg ◽  
H. Eklund ◽  
C. I. Branden
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure
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