scholarly journals Functionality of the Three-Site Ferroxidase Center of Escherichia coli Bacterial Ferritin (EcFtnA)

Biochemistry ◽  
2014 ◽  
Vol 53 (3) ◽  
pp. 483-495 ◽  
Author(s):  
F. Bou-Abdallah ◽  
H. Yang ◽  
A. Awomolo ◽  
B. Cooper ◽  
M. R. Woodhall ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ferroxidase Center ◽  
Bacterial Ferritin

scholarly journals Spectroscopic Evidence for and Characterization of a Trinuclear Ferroxidase Center in Bacterial Ferritin from Desulfovibrio vulgaris Hildenborough

2012 ◽  
Vol 134 (26) ◽  
pp. 10822-10832 ◽  
Author(s):  
Alice S. Pereira ◽  
Cristina G. Timóteo ◽  
Márcia Guilherme ◽  
Filipe Folgosa ◽  
Sunil G. Naik ◽  
...  
Keyword(s):  
Desulfovibrio Vulgaris ◽  
Spectroscopic Evidence ◽  
Ferroxidase Center ◽  
Bacterial Ferritin ◽  
Desulfovibrio Vulgaris Hildenborough

On the mineral core of ferritin-like proteins: structural and magnetic characterization

Nanoscale ◽  
2016 ◽  
Vol 8 (2) ◽  
pp. 1088-1099 ◽  
Author(s):  
A. García-Prieto ◽  
J. Alonso ◽  
D. Muñoz ◽  
L. Marcano ◽  
A. Abad Díaz de Cerio ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pyrococcus Furiosus ◽  
Magnetic Study ◽  
Magnetic Characterization ◽  
Bacterial Ferritin ◽  
Horse Spleen Ferritin ◽  
Mineral Core

We report a combined structural and magnetic study of the mineral core biomineralized by horse spleen ferritin and three prokaryotic ferritin-like proteins: bacterial ferritin and bacterioferritin from Escherichia coli and archaeal ferritin from Pyrococcus furiosus.

scholarly journals Magnetic Resonance Imaging of Tumors Colonized with Bacterial Ferritin-Expressing Escherichia coli

PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e25409 ◽  
Author(s):  
Philip J. Hill ◽  
Jochen Stritzker ◽  
Miriam Scadeng ◽  
Ulrike Geissinger ◽  
Daniel Haddad ◽  
...  
Keyword(s):  
Magnetic Resonance Imaging ◽  
Escherichia Coli ◽  
Magnetic Resonance ◽  
Resonance Imaging ◽  
Bacterial Ferritin

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

The Nature of the Intramembrane Particle

1980 ◽  
Vol 38 ◽  
pp. 688-691
Author(s):  
A.J. Verkleij
Keyword(s):  
Escherichia Coli ◽  
Tight Junction ◽  
Gap Junction ◽  
The Other ◽  
Fracture Face ◽  
Band 3 Protein ◽  
Satisfactory Explanation ◽  
Freeze Fracturing ◽  
Intramembrane Particle ◽  
Luminal Membrane

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.

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