CONFORMATIONAL CHANGES IN THE DNA MOLECULE IN SOLUTION CAUSED BY THE BINDING OF A LIGHT-SENSITIVE CATIONIC SURFACTANT

2017 ◽  
Keyword(s):  
Cationic Surfactant ◽  
Conformational Changes ◽  
Dna Molecule

Conformational changes and sequence analysis in cellulase from Aspergillus niger with cationic surfactant

Cellulose ◽  
2010 ◽  
Vol 17 (6) ◽  
pp. 1213-1225 ◽  
Author(s):  
Ali Asghar Rastegari ◽  
Abdol-Khalegh Bordbar ◽  
Vajihe Mehnati-Najafabadi
Keyword(s):  
Sequence Analysis ◽  
Aspergillus Niger ◽  
Cationic Surfactant ◽  
Conformational Changes

scholarly journals CryoEM structures of open dimers of Gyrase A in complex with DNA illuminate mechanism of strand passage

2018 ◽  
Author(s):  
Katarzyna M. Soczek ◽  
Tim Grant ◽  
Peter B. Rosenthal ◽  
Alfonso Mondragon
Keyword(s):  
Conformational Changes ◽  
Dna Cleavage ◽  
Atp Hydrolysis ◽  
Unique Type ◽  
Dna Molecule ◽  
Gyrase A ◽  
A Subunit ◽  
Important Intermediate ◽  
Dna Strand ◽  
Strand Passage

AbstractGyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage events. Structures where the transported DNA molecule (T-segment) is trapped by the A subunit have not been observed. Here we present the cryoEM structures of two oligomeric complexes of open gyrase A dimers and DNA. The protein subunits in these complexes were solved to 4 Å and 5.16 Å resolution. One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate. The structures locate the T-segment in important intermediate conformations of the catalytic cycle and provide insights into gyrase-DNA interactions and mechanism.

Conformational Transitions Control in Polynucleotide Chains by External Frequency-Modulated Exposure

2016 ◽  
Vol 845 ◽  
pp. 199-202 ◽  
Author(s):  
Farit Kabirovich Zakiryanov ◽  
Timur Rifhatovich Daukaev ◽  
Ludmila Vladimirovna Yakushevich
Keyword(s):  
Charge Transfer ◽  
Molecular Electronics ◽  
Conformational Changes ◽  
Gordon Equation ◽  
Conformational Transitions ◽  
External Exposure ◽  
Sine Gordon Equation ◽  
Dna Molecule ◽  
Close Relationship ◽  
External Frequency

Use of DNA molecules in molecular electronics is very promising. Close relationship between the charge transfer and conformational changes follows from experiment. For the theoretical descriptions of conformational transitions of DNA molecule the kink-like solutions of the modified sine-Gordon equation are mostly used. Our investigations show that the motion of the kink can be controlled by the external exposure.

Conformational changes of a DNA molecule induced by metal complexes formed in solution

2010 ◽  
Vol 52 (1) ◽  
pp. 122-133 ◽  
Author(s):  
N. A. Kasyanenko ◽  
D. A. Mukhin ◽  
I. Yu. Perevyazko
Keyword(s):  
Metal Complexes ◽  
Conformational Changes ◽  
Dna Molecule

scholarly journals CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Katarzyna M Soczek ◽  
Tim Grant ◽  
Peter B Rosenthal ◽  
Alfonso Mondragón
Keyword(s):  
Conformational Changes ◽  
Dna Cleavage ◽  
Atp Hydrolysis ◽  
Unique Type ◽  
Dna Molecule ◽  
Gyrase A ◽  
A Subunit ◽  
Important Intermediate ◽  
Dna Strand ◽  
Strand Passage

Gyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage events. Structures where the transported DNA molecule (T-segment) is trapped by the A subunit have not been observed. Here we present the cryoEM structures of two oligomeric complexes of open gyrase A dimers and DNA. The protein subunits in these complexes were solved to 4 Å and 5.2 Å resolution. One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate. The structures locate the T-segment in important intermediate conformations of the catalytic cycle and provide insights into gyrase-DNA interactions and mechanism.

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