Effects of lactose permease of Escherichia coli on the anisotropy and electrostatic surface potential of liposomes

2006 ◽  
Vol 119 (1) ◽  
pp. 101-105 ◽  
Author(s):  
Sandra Merino-Montero ◽  
M. Teresa Montero ◽  
Jordi Hernández-Borrell
Keyword(s):  
Escherichia Coli ◽  
Surface Potential ◽  
Lactose Permease ◽  
Electrostatic Surface Potential

scholarly journals Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.

1994 ◽  
Vol 269 (10) ◽  
pp. 7379-7386 ◽  
Author(s):  
P.J. Franco ◽  
R.J. Brooker
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Functional Roles

Design of a membrane protein for site-specific proteolysis: properties of engineered factor Xa protease sites in the lactose permease of Escherichia coli

Biochemistry ◽  
1995 ◽  
Vol 34 (4) ◽  
pp. 1107-1112 ◽  
Author(s):  
Miklos Sahin-Toth ◽  
Rhonda L. Dunten ◽  
H. Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Factor Xa ◽  
Lactose Permease ◽  
Site Specific

scholarly journals Topography of lactose permease from Escherichia coli.

1988 ◽  
Vol 263 (31) ◽  
pp. 15906-15914 ◽  
Author(s):  
M G Page ◽  
J P Rosenbusch
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease

Roles of Charged Residues in the Conserved Motif, G-X-X-X-D/E-R/K-X-G-[X]-R/K-R/K, of the Lactose Permease of Escherichia coli

2000 ◽  
Vol 174 (1) ◽  
pp. 31-40 ◽  
Author(s):  
N.J. Pazdernik ◽  
E.A. Matzke ◽  
A.E. Jessen-Marshall ◽  
R.J. Brooker
Keyword(s):  
Escherichia Coli ◽  
Lactose Permease ◽  
Conserved Motif ◽  
Charged Residues

scholarly journals Crystal structure of chloroplastic thioredoxin z defines a novel type-specific target recognition

2020 ◽  
Author(s):  
Théo Le Moigne ◽  
Libero Gurrieri ◽  
Pierre Crozet ◽  
Christophe H. Marchand ◽  
Mirko Zaffagnini ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Subcellular Localization ◽  
Surface Potential ◽  
Target Recognition ◽  
Chemical Mechanism ◽  
Protein Targets ◽  
Cycle Enzyme ◽  
Electrostatic Surface Potential ◽  
Trx Fold ◽  
Plant Sources

AbstractThioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant thioredoxins evolved into seven types with diverse subcellular localization and distinct protein targets selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the first crystal structure of a chloroplastic z-type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non-plant sources and is exclusively conserved in plant z-type TRXs. We show that this electronegative surface endows TRXz with a capacity to activate the photosynthetic Calvin-Benson cycle enzyme phosphoribulokinase. TRXz distinct electronegative surface thereby extends the repertoire of TRX-target recognitions.

Transport cycle of Escherichia coli lactose permease in a nonhomogeneous random walk model

2019 ◽  
Vol 99 (5) ◽  
Author(s):  
Yan B. Barreto ◽  
Matheus L. Rodrigues ◽  
Adriano M. Alencar
Keyword(s):  
Escherichia Coli ◽  
Random Walk ◽  
Random Walk Model ◽  
Lactose Permease ◽  
Transport Cycle

scholarly journals Intermolecular thiol cross-linking via loops in the lactose permease of Escherichia coli

2003 ◽  
Vol 100 (18) ◽  
pp. 10187-10192 ◽  
Author(s):  
N. Ermolova ◽  
L. Guan ◽  
H. R. Kaback
Keyword(s):  
Escherichia Coli ◽  
Cross Linking ◽  
Lactose Permease
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