scholarly journals Structural and functional studies on Salmonella typhimurium pyridoxal kinase: the first structural evidence for the formation of a Schiff base with the substrate

2021 ◽  
Vol 77 (a1) ◽  
pp. a280-a280
Author(s):  
Geeta Deka ◽  
Josyula N. Kalyani ◽  
Fathima Benazir Jahangir ◽  
Pallavi Sabharwal ◽  
H. S. Shavithri ◽  
...  
Keyword(s):  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Pyridoxal Kinase ◽  
Functional Studies

scholarly journals Structural and functional studies on Salmonella typhimurium pyridoxal kinase: the first structural evidence for the formation of Schiff base with the substrate

FEBS Journal ◽  
2019 ◽  
Vol 286 (18) ◽  
pp. 3684-3700 ◽  
Author(s):  
Geeta Deka ◽  
Josyula N. Kalyani ◽  
Fathima Benazir Jahangir ◽  
Pallavi Sabharwal ◽  
Handanahal S. Savithri ◽  
...  
Keyword(s):  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Pyridoxal Kinase ◽  
Functional Studies

Structural and Functional Studies of NirC from Salmonella typhimurium

2015 ◽  
pp. 475-497 ◽  
Author(s):  
Adriana Rycovska-Blume ◽  
Wei Lü ◽  
Susana Andrade ◽  
Klaus Fendler ◽  
Oliver Einsle
Keyword(s):  
Salmonella Typhimurium ◽  
Functional Studies

Europium and terbium Schiff base peptide complexes as potential antimicrobial agents against Salmonella typhimurium and Pseudomonas aeruginosa

2018 ◽  
Vol 72 (6) ◽  
pp. 1437-1449 ◽  
Author(s):  
Jindrich Kynicky ◽  
Vedran Milosavljevic ◽  
Pavlina Jelinkova ◽  
Yazan Haddad ◽  
Miguel Angel Merlos Rodrigo ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Antimicrobial Agents ◽  
Peptide Complexes

scholarly journals A new crystal form and antimicrobial activity of (E)-1-[3-(2-hydroxybenzylideneamino)phenyl]ethanone

2018 ◽  
Vol 74 (7) ◽  
pp. 884-888
Author(s):  
Nabila Moussa Slimane ◽  
Zakaria Bouhidel ◽  
Aouatef Cherouana
Keyword(s):  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Crystal Form ◽  
Hirshfeld Surface ◽  
Space Group ◽  
Compound C ◽  
Graph Set ◽  
Schiff Base Compound ◽  
Supramolecular Chains ◽  
Base Compound

The title Schiff base compound, C15H13NO2, crystallizes in a new crystal form in the space group P212121, which is different from the monoclinic P21/n space group reported previously [De et al. (2009). Indian J. Chem. Sect. B, 48, 595–598]. An intramolecular O—H...N hydrogen bond occurs between the hydroxy and azomethine moieties. In the crystal, molecules are linked by weak C—H...O hydrogen bonds into supramolecular chains propagating along the b-axis direction with a C(8) graph-set motif. The contribution of these two contacts in Hirshfeld surface area are around 19 and 21%, respectively. The title compound was screened for its antibacterial activity against two gram-negative (Escherichia coli and Salmonella typhimurium) and one gram-positive (Staphyloccus aureus) bacteria. The results of this study reveal that this Schiff base shows good activity against only one bacterium, i.e. Salmonella typhimurium.

scholarly journals Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli.

1996 ◽  
Vol 178 (3) ◽  
pp. 753-767 ◽  
Author(s):  
E Raux ◽  
A Lanois ◽  
F Levillayer ◽  
M J Warren ◽  
E Brody ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Vitamin B12 ◽  
Salmonella Typhimurium ◽  
Biosynthetic Genes ◽  
Functional Studies

scholarly journals Correction to: Europium and terbium Schiff base peptide complexes as potential antimicrobial agents against Salmonella typhimurium and Pseudomonas aeruginosa

2021 ◽  
Author(s):  
Jindrich Kynicky ◽  
Vedran Milosavljevic ◽  
Pavlina Jelinkova ◽  
Yazan Haddad ◽  
Miguel Angel Merlos Rodrigo ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Antimicrobial Agents ◽  
Peptide Complexes

The low-resolution 3D-structure of porin, a channel-forming protein in E. coliouter membranes

1983 ◽  
Vol 41 ◽  
pp. 440-441
Author(s):  
A. Engel ◽  
D.L. Dorset ◽  
A. Massalski ◽  
J.P. Rosenbusch
Keyword(s):  
Crystal Packing ◽  
3D Structure ◽  
Gram Negative Bacteria ◽  
Protein Ratio ◽  
Crystal Forms ◽  
Large Molecules ◽  
Functional Studies ◽  
Voltage Dependent ◽  
Planar Membranes ◽  
Hexagonal Arrays

Porins represent a group of channel forming proteins that facilitate diffusion of small solutes across the outer membrane of Gram-negative bacteria, while excluding large molecules (>650 Da). Planar membranes reconstituted from purified matrix porin (OmpF protein) trimers and phospholipids have allowed quantitative functional studies of the voltage-dependent channels and revealed concerted activation of triplets. Under the same reconstitution conditions but using high protein concentrations porin aggregated to 2D lattices suitable for electron microscopy and image processing. Depending on the lipid-to- protein ratio three different crystal packing arrangements were observed: a large (a = 93 Å) and a small (a = 79 Å) hexagonal and a rectangular (a = 79 Å b = 139 Å) form with p3 symmetry for the hexagonal arrays. In all crystal forms distinct stain filled triplet indentations could be seen and were found to be morphologically identical within a resolution of (22 Å). It is tempting to correlate stain triplets with triple channels, but the proof of this hypothesis requires an analysis of the structure in 3 dimensions.

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