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Common Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases

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https://doi.org/10.48693/295
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dc.creatorKozlova, Maria I.-
dc.creatorShalaeva, Daria N.-
dc.creatorDibrova, Daria V.-
dc.creatorMulkidjanian, Armen Y.-
dc.date.accessioned2023-04-19T13:36:52Z-
dc.date.available2023-04-19T13:36:52Z-
dc.date.issued2022-09-22-
dc.identifier.citationKozlova 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.ger
dc.identifier.urihttps://doi.org/10.48693/295-
dc.identifier.urihttps://osnadocs.ub.uni-osnabrueck.de/handle/ds-202304198709-
dc.description.abstractThe 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.eng
dc.relationhttps://doi.org/10.3390/biom12101345ger
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectWalker ATPaseeng
dc.subjectWalker A motifeng
dc.subjectWalker B motifeng
dc.subjectATPaseeng
dc.subjectRas GTPaseeng
dc.subjectarginine fingereng
dc.subjectlysine fingereng
dc.subjectABC transportereng
dc.subjectmyosineng
dc.subjectkinesineng
dc.subjectaluminum fluorideeng
dc.subjectmagnesium fluorideeng
dc.subject.ddc570 - Biowissenschaften, Biologieger
dc.titleCommon Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphataseseng
dc.typeEinzelbeitrag in einer wissenschaftlichen Zeitschrift [Article]ger
orcid.creatorhttps://orcid.org/0000-0003-0699-5064-
orcid.creatorhttps://orcid.org/0000-0002-6954-6437-
dc.identifier.doi10.3390/biom12101345-
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