Titel:	Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases
Autor(en):	Kozlova, Maria I. Shalaeva, Daria N. Dibrova, Daria V. Mulkidjanian, Armen Y.
ORCID des Autors:	https://orcid.org/0000-0003-0699-5064 https://orcid.org/0000-0002-6954-6437
Zusammenfassung:	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 comparative structural analysis of more than 3100 structures of P-loop NTPases that contain bound substrate Mg-NTPs or their analogues. We proceeded on the assumption that structural features common to these P-loop NTPases may be essential for catalysis. Our results are presented in two articles. Here, in the first, we consider the structural elements that stimulate hydrolysis. Upon interaction of P-loop NTPases with their cognate activating partners (RNA/DNA/protein domains), specific stimulatory moieties, usually Arg or Lys residues, are inserted into the catalytic site and initiate the cleavage of gamma phosphate. By analyzing a plethora of structures, we found that the only shared feature was the mechanistic interaction of stimulators with the oxygen atoms of gamma-phosphate group, capable of causing its rotation. One of the oxygen atoms of gamma phosphate coordinates the cofactor Mg ion. The rotation must pull this oxygen atom away from the Mg ion. This rearrangement should affect the properties of the other Mg ligands and may initiate hydrolysis according to the mechanism elaborated in the second article.
Bibliografische Angaben:	Kozlova M.I., Shalaeva D.N., Dibrova D.V., Mulkidjanian A.Y.: Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases. Biomolecules. 2022; 12(10):1345.
URL:	https://doi.org/10.48693/295 https://osnadocs.ub.uni-osnabrueck.de/handle/ds-202304198709
Schlagworte:	Walker ATPase; Walker A motif; Walker B motif; ATPase; Ras GTPase; arginine finger; lysine finger; ABC transporter; myosin; kinesin; aluminum fluoride; magnesium fluoride
Erscheinungsdatum:	22-Sep-2022
Lizenzbezeichnung:	Attribution 4.0 International
URL der Lizenz:	http://creativecommons.org/licenses/by/4.0/
Publikationstyp:	Einzelbeitrag in einer wissenschaftlichen Zeitschrift [Article]
Enthalten in den Sammlungen:	FB05 - Hochschulschriften Open-Access-Publikationsfonds

Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons