scholarly journals Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis

2014 ◽  
Vol 15 (2) ◽  
pp. 2223-2236 ◽  
Author(s):  
Ana Otrelo-Cardoso ◽  
Márcia da Silva Correia ◽  
Viola Schwuchow ◽  
Dmitri Svergun ◽  
Maria Romão ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Data ◽  
X Ray ◽  
Aldehyde Oxidoreductase ◽  
X Ray Crystallography

Preparation, Characterisation, Crystal Structure and Antibacterial Activity of two Bis-Schiff Bases Containing a Piperazine Ring

2018 ◽  
Vol 42 (10) ◽  
pp. 512-514
Author(s):  
Rui-bo Xu ◽  
Xiao-tian Yang ◽  
Hai-nan Li ◽  
Peng-cheng Zhao ◽  
Jiao-jiao Li ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Bacillus Subtilis ◽  
Schiff Bases ◽  
Piperazine Ring ◽  
X Ray ◽  
X Ray Crystallography ◽  
Good Antibacterial Activity

Two new bis-Schiff bases containing a piperazine ring, N,N‘-bis(4-chlorobenzylidene)- and N,N‘-bis(4-cyanobenzylidene)-1,4-bis(3-aminopropyl)piperazine, were prepared by the reaction of N,N‘-bis(3-aminopropyl)piperazine with 4-chloro- and 4-cyanobenzaldehyde, respectively. The dichloro compound was fully identified by X-ray crystallography and it exhibited good antibacterial activity against Escherichia coli, Staphylococcus aureus and Bacillus subtilis.

scholarly journals Assignment of the Ferriheme Resonances of the Low-Spin Complexes of Nitrophorins 1 and 4 by1H and13C NMR Spectroscopy:  Comparison to Structural Data Obtained from X-ray Crystallography

2007 ◽  
Vol 46 (6) ◽  
pp. 2041-2056 ◽  
Author(s):  
Tatiana Kh. Shokhireva ◽  
Andrzej Weichsel ◽  
Kevin M. Smith ◽  
Robert E. Berry ◽  
Nikolai V. Shokhirev ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Structural Data ◽  
X Ray ◽  
X Ray Crystallography

scholarly journals The canal inclusion complex of allicin with carbamide: Preparation, characterization and microbiological investigation

2005 ◽  
Vol 11 (2) ◽  
pp. 69-73 ◽  
Author(s):  
Vesna Nikolic ◽  
Mihajlo Stankovic ◽  
Ljubisa Nikolic ◽  
Dragan Cvetkovic ◽  
Agnes Kapor ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Candida Albicans ◽  
Inclusion Complex ◽  
Microbiological Investigation ◽  
X Ray ◽  
X Ray Crystallography ◽  
Bacteria And Fungi ◽  
Growth Of Bacteria

The carbamide:allicin canal inclusion complex was prepared in the solid state. The structure of the complex obtained was characterized by x-ray crystallography, infrared spectroscopy and thermogravimetric analysis. The microbiological activities of the inclusion complex and allicin were investigated and compared with respect to fungi (Candida albicans ATCC 10231 and Aspergillus niger ATCC 16404) and bacteria (Staphylococcus aureus ATCC 6538, Escherichia coli ATCC 25922, Pseudomonas aeruginosa ATCC 9027). It was found that the inclusion complex inhibited the growth of bacteria and fungi for a longer period than allicin in the free state.

scholarly journals Cocktailed fragment screening by X-ray crystallography of the antibacterial target undecaprenyl pyrophosphate synthase from Acinetobacter baumannii

2020 ◽  
Vol 76 (1) ◽  
pp. 40-46
Author(s):  
James H. Thorpe ◽  
Ian D. Wall ◽  
Robert H. Sinnamon ◽  
Amy N. Taylor ◽  
Robert A. Stavenger
Keyword(s):  
Drug Discovery ◽  
Acinetobacter Baumannii ◽  
Structural Data ◽  
X Ray ◽  
Traditional Medicines ◽  
X Ray Crystallography ◽  
Fragment Screening ◽  
Binding Pockets ◽  
Antibacterial Target ◽  
Robustness Check

Direct soaking of protein crystals with small-molecule fragments grouped into complementary clusters is a useful technique when assessing the potential of a new crystal system to support structure-guided drug discovery. It provides a robustness check prior to any extensive crystal screening, a double check for assay binding cutoffs and structural data for binding pockets that may or may not be picked out in assay measurements. The structural output from this technique for three novel fragment molecules identified to bind to the antibacterial target Acinetobacter baumannii undecaprenyl pyrophosphate synthase are reported, and the different physicochemical requirements of a successful antibiotic are compared with traditional medicines.

scholarly journals Structure, Folding and Stability of Nucleoside Diphosphate Kinases

2020 ◽  
Vol 21 (18) ◽  
pp. 6779
Author(s):  
Florian Georgescauld ◽  
Yuyu Song ◽  
Alain Dautant
Keyword(s):  
Catalytic Mechanism ◽  
Catalytic Efficiency ◽  
Structural Data ◽  
Membrane Remodeling ◽  
Oligomeric Proteins ◽  
X Ray ◽  
X Ray Crystallography ◽  
Assembly Structure ◽  
Nucleoside Diphosphate Kinases ◽  
Cytoskeleton Dynamics

Nucleoside diphosphate kinases (NDPK) are oligomeric proteins involved in the synthesis of nucleoside triphosphates. Their tridimensional structure has been solved by X-ray crystallography and shows that individual subunits present a conserved ferredoxin fold of about 140 residues in prokaryotes, archaea, eukaryotes and viruses. Monomers are functionally independent from each other inside NDPK complexes and the nucleoside kinase catalytic mechanism involves transient phosphorylation of the conserved catalytic histidine. To be active, monomers must assemble into conserved head to tail dimers, which further assemble into hexamers or tetramers. The interfaces between these oligomeric states are very different but, surprisingly, the assembly structure barely affects the catalytic efficiency of the enzyme. While it has been shown that assembly into hexamers induces full formation of the catalytic site and stabilizes the complex, it is unclear why assembly into tetramers is required for function. Several additional activities have been revealed for NDPK, especially in metastasis spreading, cytoskeleton dynamics, DNA binding and membrane remodeling. However, we still lack the high resolution structural data of NDPK in complex with different partners, which is necessary for deciphering the mechanism of these diverse functions. In this review we discuss advances in the structure, folding and stability of NDPKs.

Ru-Based CO releasing molecules with azole ligands: interaction with proteins and the CO release mechanism disclosed by X-ray crystallography

2017 ◽  
Vol 46 (29) ◽  
pp. 9621-9629 ◽  
Author(s):  
Nicola Pontillo ◽  
Giarita Ferraro ◽  
Luigi Messori ◽  
Gabriella Tamasi ◽  
Antonello Merlino
Keyword(s):  
Structural Data ◽  
Release Mechanism ◽  
X Ray ◽  
X Ray Crystallography

Structural data on the adducts formed upon reaction of Ru-based CO releasing molecules containing azole ligands with model proteins are reported.

scholarly journals Synergy of Streptogramin Antibiotics Occurs Independently of Their Effects on Translation

2014 ◽  
Vol 58 (9) ◽  
pp. 5269-5279 ◽  
Author(s):  
Jonas Noeske ◽  
Jian Huang ◽  
Nelson B. Olivier ◽  
Robert A. Giacobbe ◽  
Mark Zambrowski ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Activity ◽  
Pathogenic Bacteria ◽  
Type A ◽  
Type B ◽  
Content Type ◽  
X Ray ◽  
X Ray Crystallography ◽  
70S Ribosome ◽  
Rapid Hydrolysis

ABSTRACTStreptogramin antibiotics are divided into types A and B, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin) and NXL 103 (type A, flopristin; type B, linopristin) with theEscherichia coli70S ribosome by X-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. The streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that the synergistic antimicrobial activity of streptogramins can occur independently of the effects of streptogramin on translation.

The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography

1994 ◽  
Vol 235 (1) ◽  
pp. 47-52 ◽  
Author(s):  
L. Anders Svensson ◽  
Brian P. Surin ◽  
Nicholas E. Dixon ◽  
Michael D. Spangfort
Keyword(s):  
Escherichia Coli ◽  
X Ray ◽  
X Ray Crystallography
Sign in / Sign up

Export Citation Format

Share Document