X‐ray Crystal Structure of Agmatinase from Escherichia coli

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Syed Fardin Ahmed ◽  
Iva Chitrakar ◽  
Andrew T. Torelli ◽  
Jarrod B. French
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
X Ray

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 X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC)

2014 ◽  
Vol 445 (2) ◽  
pp. 439-444 ◽  
Author(s):  
J. Domingo Meza-Aguilar ◽  
Petra Fromme ◽  
Alfredo Torres-Larios ◽  
Guillermo Mendoza-Hernández ◽  
Ulises Hernandez-Chiñas ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Passenger Domain ◽  
X Ray

scholarly journals The X-Ray Crystal Structure of Escherichia coli Succinic Semialdehyde Dehydrogenase; Structural Insights into NADP+/Enzyme Interactions

PLoS ONE ◽  
2010 ◽  
Vol 5 (2) ◽  
pp. e9280 ◽  
Author(s):  
Christopher G. Langendorf ◽  
Trevor L. G. Key ◽  
Gustavo Fenalti ◽  
Wan-Ting Kan ◽  
Ashley M. Buckle ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Succinic Semialdehyde ◽  
Succinic Semialdehyde Dehydrogenase ◽  
X Ray ◽  
Semialdehyde Dehydrogenase ◽  
Structural Insights

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 High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE

2020 ◽  
Vol 76 (9) ◽  
pp. 414-421
Author(s):  
Liyana Azmi ◽  
Eilis C. Bragginton ◽  
Ian T. Cadby ◽  
Olwyn Byron ◽  
Andrew J. Roe ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Aldehyde Dehydrogenase ◽  
X Ray ◽  
X Ray Scattering ◽  
Bacterial Enzyme ◽  
High Resolution Structure ◽  
Resolution Structure

The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 Å resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.

scholarly journals X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 Å resolution

Structure ◽  
1999 ◽  
Vol 7 (9) ◽  
pp. 1155-1166 ◽  
Author(s):  
Chenglong Li ◽  
T Joseph Kappock ◽  
JoAnne Stubbe ◽  
Todd M Weaver ◽  
Steven E Ealick
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Biosynthetic Pathway ◽  
X Ray

scholarly journals Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases

2020 ◽  
Vol 76 (3) ◽  
pp. 291-301 ◽  
Author(s):  
Jack A. Dunkle ◽  
Michael R. Bruno ◽  
Patrick A. Frantom
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Sequence Analysis ◽  
Active Site ◽  
Resting State ◽  
Sulfur Source ◽  
Structural Elements ◽  
Cysteine Desulfurase ◽  
X Ray

Cysteine serves as the sulfur source for the biosynthesis of Fe–S clusters and thio-cofactors, molecules that are required for core metabolic processes in all organisms. Therefore, cysteine desulfurases, which mobilize sulfur for its incorporation into thio-cofactors by cleaving the Cα—S bond of cysteine, are ubiquitous in nature. SufS, a type 2 cysteine desulfurase that is present in plants and microorganisms, mobilizes sulfur from cysteine to the transpersulfurase SufE to initiate Fe–S biosynthesis. Here, a 1.5 Å resolution X-ray crystal structure of the Escherichia coli SufS homodimer is reported which adopts a state in which the two monomers are rotated relative to their resting state, displacing a β-hairpin from its typical position blocking transpersulfurase access to the SufS active site. A global structure and sequence analysis of SufS family members indicates that the active-site β-hairpin is likely to require adjacent structural elements to function as a β-latch regulating access to the SufS active site.

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