Repository logo
 
Publication

Characterization of Danio rerio Mn2+-Dependent ADP-Ribose/CDP-Alcohol Diphosphatase, the Structural Prototype of the ADPRibase-Mn-Like Protein Family

2012Journal article Open access
Simple item page
dc.contributor.authorRodrigues, Joaquim Rui
dc.contributor.authorFernández, Ascensión
dc.contributor.authorCanales, José
dc.contributor.authorCabezas, Alicia
dc.contributor.authorRibeiro, João Meireles
dc.contributor.authorCostas, María Jesús
dc.contributor.authorCameselle, José Carlos
dc.date.accessioned2018-02-07T10:14:15Z
dc.date.available2018-02-07T10:14:15Z
dc.date.issued2012
dc.description.abstractThe ADPRibase-Mn-like protein family, that belongs to the metallo-dependent phosphatase superfamily, has different functional and structural prototypes. The functional one is the Mn(2+)-dependent ADP-ribose/CDP-alcohol diphosphatase from Rattus norvegicus, which is essentially inactive with Mg(2+) and active with low micromolar Mn(2+) in the hydrolysis of the phosphoanhydride linkages of ADP-ribose, CDP-alcohols and cyclic ADP-ribose (cADPR) in order of decreasing efficiency. The structural prototype of the family is a Danio rerio protein with a known crystallographic structure but functionally uncharacterized. To estimate the structure-function correlation with the same protein, the activities of zebrafish ADPRibase-Mn were studied. Differences between zebrafish and rat enzymes are highlighted. The former showed a complex activity dependence on Mn(2+), significant (≈25%) Mg(2+)-dependent activity, but was almost inactive on cADPR (150-fold less efficient than the rat counterpart). The low cADPR hydrolase activity agreed with the zebrafish genome lacking genes coding for proteins with significant homology with cADPR-forming enzymes. Substrate-docking to zebrafish wild-type protein, and characterization of the ADPRibase-Mn H97A mutant pointed to a role of His-97 in catalysis by orientation, and to a bidentate water bridging the dinuclear metal center as the potential nucleophile. Finally, three structural elements that delimit the active site entrance in the zebrafish protein were identified as unique to the ADPRibase-Mn-like family within the metallo-dependent phosphatase superfamily.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1371/journal.pone.0042249pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.8/3008
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAdenosine Diphosphate Ribosept_PT
dc.subjectAnimalspt_PT
dc.subjectBinding Sitespt_PT
dc.subjectCatalytic Domainpt_PT
dc.subjectCyclic AMPpt_PT
dc.subjectCytidine Diphosphatept_PT
dc.subjectEnzyme Activationpt_PT
dc.subjectHydrogen-Ion Concentrationpt_PT
dc.subjectMagnesiumpt_PT
dc.subjectManganesept_PT
dc.subjectMolecular Docking Simulationpt_PT
dc.subjectMutationpt_PT
dc.subjectPyrophosphatasespt_PT
dc.subjectRatspt_PT
dc.subjectSubstrate Specificitypt_PT
dc.subjectZebrafish Proteinspt_PT
dc.subjectZebrafishpt_PT
dc.titleCharacterization of Danio rerio Mn2+-Dependent ADP-Ribose/CDP-Alcohol Diphosphatase, the Structural Prototype of the ADPRibase-Mn-Like Protein Familypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue7pt_PT
oaire.citation.startPagee42249pt_PT
oaire.citation.titlePLoS ONEpt_PT
oaire.citation.volume7pt_PT
person.familyNameRodrigues
person.givenNameJoaquim Rui
person.identifier.ciencia-id9018-0B83-E2C6
person.identifier.orcid0000-0002-9756-1124
person.identifier.ridL-4137-2014
person.identifier.scopus-author-id10242931100
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication52f6ffb2-43e9-4f78-b414-dbac46f80305
relation.isAuthorOfPublication.latestForDiscovery52f6ffb2-43e9-4f78-b414-dbac46f80305

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Rodrigues_et_al-2012-PLOS_ONE.pdf
Size:
2.35 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.32 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

ESTG - Artigos em revistas internacionais