Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism

Metallomics ◽  
2016 ◽  
Vol 8 (3) ◽  
pp. 327-336 ◽  
Author(s):  
H. G. Colaço ◽  
P. E. Santo ◽  
P. M. Matias ◽  
T. M. Bandeiras ◽  
J. B. Vicente
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
Binding Mechanism ◽  
Cadmium Resistance ◽  
Structural Insights

Structural-functional platform unravels new roles for ZinT in cobalt, mercury and cadmium resistance, providing clues into the metal binding mechanism.

scholarly journals Kinetic Analysis of the Metal Binding Mechanism of Escherichia coli Manganese Superoxide Dismutase

2006 ◽  
Vol 90 (2) ◽  
pp. 598-607 ◽  
Author(s):  
Mei M. Whittaker ◽  
Kazunori Mizuno ◽  
Hans Peter Bächinger ◽  
James W. Whittaker
Keyword(s):  
Escherichia Coli ◽  
Superoxide Dismutase ◽  
Kinetic Analysis ◽  
Metal Binding ◽  
Manganese Superoxide Dismutase ◽  
Binding Mechanism ◽  
Manganese Superoxide

scholarly journals Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility–mass spectrometry

2019 ◽  
Vol 476 (21) ◽  
pp. 3125-3139 ◽  
Author(s):  
Daniel Shiu-Hin Chan ◽  
Jeannine Hess ◽  
Elen Shaw ◽  
Christina Spry ◽  
Robert Starley ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Structural Biology ◽  
Ion Mobility ◽  
Biosynthetic Pathway ◽  
Screening Tool ◽  
Native Mass Spectrometry ◽  
Ion Mobility Mass Spectrometry ◽  
E Coli ◽  
Structural Insights

Abstract CoaBC, part of the vital coenzyme A biosynthetic pathway in bacteria, has recently been validated as a promising antimicrobial target. In this work, we employed native ion mobility–mass spectrometry to gain structural insights into the phosphopantothenoylcysteine synthetase domain of E. coli CoaBC. Moreover, native mass spectrometry was validated as a screening tool to identify novel inhibitors of this enzyme, highlighting the utility and versatility of this technique both for structural biology and for drug discovery.

scholarly journals Metal-binding chimeric antibodies expressed in Escherichia coli.

1992 ◽  
Vol 89 (20) ◽  
pp. 9754-9758 ◽  
Author(s):  
J. R. Sawyer ◽  
P. W. Tucker ◽  
F. R. Blattner
Keyword(s):  
Escherichia Coli ◽  
Metal Binding ◽  
Chimeric Antibodies

Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli

2021 ◽  
Vol 118 (50) ◽  
pp. e2114013118
Author(s):  
Tamara N. Grund ◽  
Melanie Radloff ◽  
Di Wu ◽  
Hojjat G. Goojani ◽  
Luca F. Witte ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pathogenic Bacteria ◽  
Reduction Rate ◽  
Structural Diversity ◽  
Multidrug Resistant ◽  
E Coli ◽  
Structural And Functional Properties ◽  
Oxygen Reductase ◽  
General Architecture ◽  
Structural Insights

The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome bd-type oxygen reductase is a critical survival factor utilized by pathogenic bacteria during infection, proliferation and the transition from acute to chronic states. Escherichia coli encodes for two cytochrome bd isoforms that are both involved in respiration under oxygen limited conditions. Mechanistic and structural differences between cydABX (Ecbd-I) and appCBX (Ecbd-II) operon encoded cytochrome bd variants have remained elusive in the past. Here, we demonstrate that cytochrome bd-II catalyzes oxidation of benzoquinols while possessing additional specificity for naphthoquinones. Our data show that although menaquinol-1 (MK1) is not able to directly transfer electrons onto cytochrome bd-II from E. coli, it has a stimulatory effect on its oxygen reduction rate in the presence of ubiquinol-1. We further determined cryo-EM structures of cytochrome bd-II to high resolution of 2.1 Å. Our structural insights confirm that the general architecture and substrate accessible pathways are conserved between the two bd oxidase isoforms, but two notable differences are apparent upon inspection: (i) Ecbd-II does not contain a CydH-like subunit, thereby exposing heme b595 to the membrane environment and (ii) the AppB subunit harbors a structural demethylmenaquinone-8 molecule instead of ubiquinone-8 as found in CydB of Ecbd-I. Our work completes the structural landscape of terminal respiratory oxygen reductases of E. coli and suggests that structural and functional properties of the respective oxidases are linked to quinol-pool dependent metabolic adaptations in E. coli.

scholarly journals Structural insights into the mechanism of c-di-GMP–bound YcgR regulating flagellar motility in Escherichia coli

2019 ◽  
Vol 295 (3) ◽  
pp. 808-821 ◽  
Author(s):  
Yan-Jie Hou ◽  
Wen-Si Yang ◽  
Yuan Hong ◽  
Ying Zhang ◽  
Da-Cheng Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Motor Proteins ◽  
Flagellar Motor ◽  
Bacterial Survival ◽  
Flagellar Motility ◽  
Surface Attachment ◽  
Bacterial Surface ◽  
Motility Regulation ◽  
Survival And Growth ◽  
Structural Insights

The motile-sessile transition is critical for bacterial survival and growth. Cyclic-di-GMP (c-di-GMP) plays a central role in controlling this transition and regulating biofilm formation via various effectors. As an effector of c-di-GMP in Escherichia coli and related species, the PilZ domain–containing protein YcgR responds to elevated c-di-GMP concentrations and acts on the flagellar motor to suppress bacterial motility in a brakelike fashion, which promotes bacterial surface attachment. To date, several target proteins within the motor, MotA, FliG, and FliM, along with different regulatory mechanisms have been reported. However, how YcgR acts on these components remains unclear. Here, we report that activated YcgR stably binds to MotA at the MotA-FliG interface and thereby regulates bacterial swimming. Biochemical and structural analyses revealed that c-di-GMP rearranges the PilZ domain configuration, resulting in the formation of a MotA-binding patch consisting of an RXXXR motif and the C-tail helix α3. Moreover, we noted that a conserved region in the YcgR-N domain, which is independent of MotA interaction, is necessary for motility regulation. On the basis of these findings, we infer that the YcgR-N domain is required for activity on other motor proteins. We propose that activated YcgR appends to MotA via its PilZ domain and thereby interrupts the MotA-FliG interaction and simultaneously interacts with other motor proteins via its YcgR-N domain to inhibit flagellar motility. Our findings suggest that the mode of interaction between YcgR and motor proteins may be shared by other PilZ family proteins.

Expression of Bacillus stearothermophilus LV Cadmium Resistance Genes in Escherichia coli Causes Hypersensitivity to Cadmium Chloride

2002 ◽  
Vol 45 (3) ◽  
pp. 187-190 ◽  
Author(s):  
Mayte del C. Nerey ◽  
Sergio E. Pichuantes ◽  
Claudia P. Saavedra ◽  
Manuel A. Araya ◽  
Juan C. Tantaleán ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Resistance Genes ◽  
Cadmium Chloride ◽  
Bacillus Stearothermophilus ◽  
Cadmium Resistance
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