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

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dc.contributor.authorKozlova, I, Maria
dc.contributor.authorShalaeva, Daria N.
dc.contributor.authorDibrova, V, Daria
dc.contributor.authorMulkidjanian, Armen Y.
dc.date.accessioned2023-02-17T11:34:00Z-
dc.date.available2023-02-17T11:34:00Z-
dc.date.issued2022
dc.identifier.urihttp://osnascholar.ub.uni-osnabrueck.de/handle/unios/65408-
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.
dc.description.sponsorshipDFG; DAAD; Osnabrueck University; The research was supported by DFG, DAAD, and Osnabrueck University (the EvoCell Program and Open Access Publishing Fund).
dc.language.isoen
dc.publisherMDPI
dc.relation.ispartofBIOMOLECULES
dc.subjectABC transporter
dc.subjectALUMINUM FLUORIDE
dc.subjectarginine finger
dc.subjectARGININE-FINGER
dc.subjectATP HYDROLYSIS
dc.subjectATPase
dc.subjectBINDING
dc.subjectBiochemistry & Molecular Biology
dc.subjectCHROMOSOME SEGREGATION
dc.subjectG DOMAIN
dc.subjectGTPASE-ACTIVATING PROTEIN
dc.subjectkinesin
dc.subjectlysine finger
dc.subjectmagnesium fluoride
dc.subjectmyosin
dc.subjectRas GTPase
dc.subjectSTRUCTURAL BASIS
dc.subjectTRANSITION-STATE ANALOG
dc.subjectWalker A motif
dc.subjectWalker ATPase
dc.subjectWalker B motif
dc.subjectX-RAY
dc.titleCommon Patterns of Hydrolysis Initiation in P-loop Fold Nucleoside Triphosphatases
dc.typejournal article
dc.identifier.doi10.3390/biom12101345
dc.identifier.isiISI:000874179600001
dc.description.volume12
dc.description.issue10
dc.contributor.orcid0000-0003-0699-5064
dc.identifier.eissn2218-273X
dc.publisher.placeST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
dcterms.isPartOf.abbreviationBiomolecules
dcterms.oaStatusgold, Green Published, Green Submitted
local.import.remainsaffiliations : University Osnabruck; University Osnabruck; Lomonosov Moscow State University
local.import.remainsweb-of-science-index : Science Citation Index Expanded (SCI-EXPANDED)
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