Maria Kozlova

Maria Kozlova
  • PhD Student at Osnabrück University

About

11
Publications
2,073
Reads
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92
Citations
Current institution
Osnabrück University
Current position
  • PhD Student
Education
September 2012 - June 2018
Lomonosov Moscow State University
Field of study
  • Bioengineering and Bioinformatics

Publications

Publications (11)
Article
Full-text available
To clarify the obscure hydrolysis mechanism of ubiquitous P-loop-fold nucleoside triphosphatases (Walker NTPases), we analysed the structures of 3136 catalytic sites with bound Mg-NTP complexes or their analogues. Our results are presented in two articles; here, in the second of them, we elucidated whether the Walker A and Walker B sequence motifs—...
Article
Full-text available
The P-loop fold nucleoside triphosphate (NTP) hydrolases (also known as Walker NTPases) function as ATPases, GTPases, and ATP synthases, are often of medical importance, and represent one of the largest and evolutionarily oldest families of enzymes. There is still no consensus on their catalytic mechanism. To clarify this, we performed the first co...
Preprint
In ubiquitous P-loop fold n ucleoside t ri p hosphatases (also known as Walker NTPases), hydrolysis of ATP or GTP is initiated by interaction with an activating partner (usually another protein domain), which is accompanied by insertion of stimulatory moiety(ies) (usually arginine or lysine residues) into the catalytic site. After inspecting over 3...
Preprint
Full-text available
Although P-loop fold n ucleoside tri p hosphatases (also known as Walker NTPases) are ubiquitous, their catalytic mechanism remains obscure. Based on a comparative structural analysis of 3136 Mg-NTP-containing catalytic sites, we propose a common scheme of activated catalysis for P-loop NTPases where a hydrogen bond (H-bond) between the strictly co...
Article
Full-text available
The ATP hydrolysis transition state of motor proteins is a weakly populated protein state that can be stabilized and investigated by replacing ATP with chemical mimics. We present atomic-level structural and dynamic insights on a state created by ADP aluminum fluoride binding to the bacterial DnaB helicase from Helicobacter pylori . We determined t...
Preprint
Full-text available
The ATP hydrolysis transition state of motor proteins is a weakly populated protein state that can be stabilized and investigated by replacing ATP with chemical mimics. We present atomic-level structural and dynamic insights on a state created by ADP aluminum fluoride binding to the bacterial DnaB helicase from Helicobacter pylori. We determined th...
Article
Full-text available
In 1986, Vladimir Skulachev and his colleagues coined the term “Sodium World” for the group of diverse organisms with sodium (Na)-based bioenergetics. Albeit only few such organisms had been discovered by that time, the authors insightfully noted that “the great taxonomic variety of organisms employing the Na-cycle points to the ubiquitous distribu...
Article
Full-text available
Nucleoside triphosphates (NTPs) are used as chemical energy source in a variety of cell systems. Structural snapshots along the NTP hydrolysis reaction coordinate are typically obtained by adding stable, nonhydrolyzable adenosine triphosphate (ATP) -analogues to the proteins, with the goal to arrest a state that mimics as closely as possible a phys...

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