uu.seUppsala universitets publikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG
Department of Biochemistry and Biophysics, Stockholm Center for Biomembrane Research, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden. (Helen Wang)
2009 (engelsk)Inngår i: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 106, nr 34, s. 14247-14252Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

ADP-ribosylation is a ubiquitous regulatory posttranslational modi- fication involved in numerous key processes such as DNA repair, transcription, cell differentiation, apoptosis, and the pathogenic mechanism of certain bacterial toxins. Despite the importance of this reversible process, very little is known about the structure and mechanism of the hydrolases that catalyze removal of the ADP-ribose moiety. In the phototrophic bacterium Rhodospirillum rubrum, dini- trogenase reductase-activating glycohydrolase (DraG), a dimanga- nese enzyme that reversibly associates with the cell membrane, is a key player in the regulation of nitrogenase activity. DraG has long served as a model protein for ADP-ribosylhydrolases. Here, we present the crystal structure of DraG in the holo and ADP-ribose bound forms. We also present the structure of a reaction intermediate analogue and propose a detailed catalytic mechanism for protein de-ADP-ribosylation involving ring opening of the substrate ribose. In addition, the particular manganese coordination in DraG suggests a rationale for the enzyme’s preference for manganese over magne- sium, although not requiring a redox active metal for the reaction.

sted, utgiver, år, opplag, sider
2009. Vol. 106, nr 34, s. 14247-14252
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-382890DOI: 10.1073/pnas.0905906106ISI: 000269295100017PubMedID: 19706507OAI: oai:DiVA.org:uu-382890DiVA, id: diva2:1313707
Tilgjengelig fra: 2019-05-06 Laget: 2019-05-06 Sist oppdatert: 2019-05-09bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMed

Personposter BETA

Wang, Helen

Søk i DiVA

Av forfatter/redaktør
Wang, Helen
I samme tidsskrift
Proceedings of the National Academy of Sciences of the United States of America

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 5 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf