Genetic and structural characterization of the bacterioferritin of Escherichia coli

1990 ◽  
Vol 18 (4) ◽  
pp. 658-659 ◽  
Author(s):  
SIMON C. ANDREWS ◽  
JOHN M. A. SMITH ◽  
JOHN R. GUEST ◽  
PAULINE M. HARRISON
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization

Iron–sulfur repair YtfE protein from Escherichia coli: structural characterization of the di-iron center

2008 ◽  
Vol 13 (5) ◽  
pp. 765-770 ◽  
Author(s):  
Smilja Todorovic ◽  
Marta C. Justino ◽  
Gerd Wellenreuther ◽  
Peter Hildebrandt ◽  
Daniel H. Murgida ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Iron Sulfur ◽  
Iron Center

scholarly journals Structural Characterization of U*-1915 in Domain IV from Escherichia Coli 23S Ribosomal RNA as 3-Methylpseudouridine

1996 ◽  
Vol 24 (4) ◽  
pp. 688-693 ◽  
Author(s):  
J. A. Kowalak ◽  
E. Bruenger ◽  
T. Hashizume ◽  
J. M. Peltier ◽  
J. Ofengand ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Structural Characterization ◽  
23S Ribosomal Rna

scholarly journals Biochemical and Structural Characterization of the Subclass B1 Metallo-β-Lactamase VIM-4

2010 ◽  
Vol 55 (3) ◽  
pp. 1248-1255 ◽  
Author(s):  
Patricia Lassaux ◽  
Daouda A. K. Traoré ◽  
Elodie Loisel ◽  
Adrien Favier ◽  
Jean-Denis Docquier ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Thermal Stability ◽  
Pseudomonas Aeruginosa ◽  
Structural Characterization ◽  
Catalytic Efficiency ◽  
X Ray ◽  
Stabilizing Effect ◽  
Loop 2

ABSTRACTThe metallo-β-lactamase VIM-4, mainly found inPseudomonas aeruginosaorAcinetobacter baumannii, was produced inEscherichia coliand characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn2+at concentrations ranging from 0.4 to 100 μM showed that VIM-4 exhibits a kinetic profile similar to the profiles of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin, and imipenem and is less active than VIM-2 against ampicillin and meropenem. The crystal structure of the dizinc form of VIM-4 was solved at 1.9 Å. The sole difference between VIM-4 and VIM-1 is found at residue 228, which is Ser in VIM-1 and Arg in VIM-4. This substitution has a major impact on the VIM-4 catalytic efficiency compared to that of VIM-1. In contrast, the differences between VIM-2 and VIM-4 seem to be due to a different position of the flapping loop and two substitutions in loop 2. Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn2+ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure.

scholarly journals Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli

1993 ◽  
Vol 211 (1-2) ◽  
pp. 347-355 ◽  
Author(s):  
Rosaria ARCONE ◽  
Giuseppina ARPAIA ◽  
Margherita RUOPPOLO ◽  
Antonio MALORNI ◽  
Piero PUCCI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Biologically Active

scholarly journals Correction to Structural Characterization of a Model Gram-Negative Bacterial Surface Using Lipopolysaccharides from Rough Strains of Escherichia coli

2014 ◽  
Vol 15 (8) ◽  
pp. 3213-3213
Author(s):  
Anton P. Le Brun ◽  
Luke A. Clifton ◽  
Candice E. Halbert ◽  
Binhua Lin ◽  
Mati Meron ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Characterization ◽  
Gram Negative ◽  
Bacterial Surface
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