sh.sePublikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • harvard-anglia-ruskin-university
  • apa-old-doi-prefix.csl
  • 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
Glutaredoxin-3 from Escherichia coli: Amino acid sequence, H-1 and N-15 NMR assignments, and structural analysis
Karolinska Institutet.ORCID-id: 0000-0002-3049-967X
Vise andre og tillknytning
1996 (engelsk)Inngår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 271, nr 12, s. 6736-6745Artikkel i tidsskrift (Fagfellevurdert) Published
Resurstyp
Text
Abstract [en]

The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily. in addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys(65)) corresponding to one of the two non-active site (or structural) cysteine residues present in mammalian glutaredoxins. The sequence-specific H-1 and N-15 nuclear magnetic resonance assignments of reduced Grx3 have been obtained. From a combined analysis of chemical shifts, (3)J(HN alpha) coupling constants, sequential and medium range NOEs, and amide proton exchange rates, the secondary structure of reduced Grx3 was determined and found to be very similar to that inferred from amino acid sequence comparison to homologous proteins. The consequences of the proposed structural similarity to Grx1 are that Grx3, while possessing a largely intact GSH binding cleft, would have a very different spatial distribution of charged residues, most notably surrounding the active site cysteine residues and occurring in the proposed hydrophobic protein-protein interaction area. These differences may contribute to the observed very low K-cat of Grx3 as a reductant of insulin disulfides or as a hydrogen donor for ribonucleotide reductase. Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grxl display large functional differences in in vitro protein disulfide oxide-reduction reactions.

sted, utgiver, år, opplag, sider
1996. Vol. 271, nr 12, s. 6736-6745
Emneord [en]
3-dimensional structure, deoxyribonucleotides, glutathione-dependent synthesis, human thioredoxin, mixed disulfide, proteins, proton proton distances, purification, secondary structure determination, spectroscopy
HSV kategori
Identifikatorer
URN: urn:nbn:se:sh:diva-28994DOI: 10.1074/jbc.271.12.6736ISI: A1996UB15700029OAI: oai:DiVA.org:sh-28994DiVA, id: diva2:892178
Merknad

Times Cited: 28 Article English Cited References Count: 62 Ub157

Tilgjengelig fra: 2016-01-08 Laget: 2016-01-07 Sist oppdatert: 2017-12-01bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekst

Personposter BETA

Berndt, Kurt D

Søk i DiVA

Av forfatter/redaktør
Berndt, Kurt D
I samme tidsskrift
Journal of Biological Chemistry

Søk utenfor DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric

doi
urn-nbn
Totalt: 90 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • harvard-anglia-ruskin-university
  • apa-old-doi-prefix.csl
  • 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