Alterations in the structure and function of Escherichia coli. Alkaline phosphatase due to zinc ion binding

Biochemistry ◽  
1969 ◽  
Vol 8 (2) ◽  
pp. 588-593 ◽  
Author(s):  
Jacqueline A. Reynolds ◽  
Milton J. Schlesinger
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Zinc Ion ◽  
Structure And Function ◽  
Ion Binding ◽  
And Function ◽  
Zinc Ion Binding

scholarly journals Micro-analysis of pure deoxyribonucleic acid-dependent ribonucleic acid polymerase from Escherichia coli. Action of heparin and rifampicin on structure and function

1970 ◽  
Vol 117 (3) ◽  
pp. 623-631 ◽  
Author(s):  
Volker Neuhoff ◽  
Wolf-Bernhard Schill ◽  
Hans Sternbach
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Rna Synthesis ◽  
Deoxyribonucleic Acid ◽  
Structure And Function ◽  
Disc Electrophoresis ◽  
Inhibitory Mechanism ◽  
And Function ◽  
Micro Analysis ◽  
Template Complex

By using micro disc electrophoresis and micro-diffusion techniques, the interaction of pure DNA-dependent RNA polymerase (EC 2.7.7.6) from Escherichia coli with the template, the substrates and the inhibitors heparin and rifampicin was investigated. The following findings were obtained: (1) heparin converts the 24S and 18S particles of the polymerase into the 13S form; (2) heparin inhibits RNA synthesis by dissociating the enzyme–template complex; (3) rifampicin does not affect the attachment of heparin to the enzyme; (4) the substrates ATP and UTP are bound by enzyme loaded with rifampicin; (5) rifampicin is bound by an enzyme–template complex to the same extent as by an RNA-synthesizing enzyme–template complex. From this it is concluded that the mechanism of the inhibition of RNA synthesis by rifampicin is radically different from that by heparin. As a working hypothesis to explain the inhibitory mechanism of rifampicin, it is assumed that it becomes very firmly attached to a position close to the synthesizing site and only blocks this when no synthesis is in progress.

scholarly journals Influence of High Pressure on the Dimerization of ToxR, a Protein Involved in Bacterial Signal Transduction

2008 ◽  
Vol 74 (24) ◽  
pp. 7821-7823 ◽  
Author(s):  
Kai Linke ◽  
Nagarajan Periasamy ◽  
Matthias Ehrmann ◽  
Roland Winter ◽  
Rudi F. Vogel
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
High Pressure ◽  
Structure And Function ◽  
Transmembrane Segments ◽  
Bacterial Signal Transduction ◽  
Reporter Strains ◽  
And Function ◽  
First Time

ABSTRACT High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.

scholarly journals The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit.

1993 ◽  
Vol 268 (36) ◽  
pp. 27094-27099
Author(s):  
B Stolz ◽  
M Huber ◽  
Z Marković-Housley ◽  
B Erni
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
And Function

scholarly journals Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Translation Initiation ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Ion Binding ◽  
Binding Interface ◽  
Zinc Binding Site ◽  
Reading Frames ◽  
Zinc Ion Binding

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR’s MCT-1–binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function

2007 ◽  
Vol 1 (1) ◽  
pp. 89-91 ◽  
Author(s):  
Julien Boudet ◽  
Anne Chouquet ◽  
Aicha Chahboune ◽  
Cécile Giustini ◽  
Bernard Joris ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Resonance Assignments ◽  
Structure And Function ◽  
Unknown Structure ◽  
And Function
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