Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • 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
Structure and activity of the Streptococcus pyogenes family GH1 6-phospho-beta-glucosidase SPy1599
KTH, Skolan för bioteknologi (BIO), Glykovetenskap.
KTH, Skolan för bioteknologi (BIO), Glykovetenskap.
Vise andre og tillknytning
2013 (engelsk)Inngår i: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 69, s. 16-23Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The group A streptococcus Streptococcus pyogenes is the causative agent of a wide spectrum of invasive infections, including necrotizing fasciitis, scarlet fever and toxic shock syndrome. In the context of its carbohydrate chemistry, it is interesting that S. pyogenes (in this work strain M1 GAS SF370) displays a spectrum of oligosaccharide-processing enzymes that are located in close proximity on the genome but that the in vivo function of these proteins remains unknown. These proteins include different sugar transporters (SPy1593 and SPy1595), both GH125 alpha-1,6- and GH38 alpha-1,3-mannosidases (SPy1603 and SPy1604), a GH84 beta-hexosaminidase (SPy1600) and a putative GH2 beta-galactosidase (SPy1586), as well as SPy1599, a family GH1 'putative beta-glucosidase'. Here, the solution of the three-dimensional structure of SPy1599 in a number of crystal forms complicated by unusual crystallographic twinning is reported. The structure is a classical (beta/alpha)(g)-barrel, consistent with CAZy family GH1 and other members of the GH-A clan. SPy1599 has been annotated in sequence depositions as a beta-glucosidase (EC 3.2.1.21), but no such activity could be found; instead, three-dimensional structural overlaps with other enzymes of known function suggested that SPy1599 contains a phosphate-binding pocket in the active site and has possible 6-phospho-beta-glycosidase activity. Subsequent kinetic analysis indeed showed that SPy1599 has 6-phospho-beta-glucosidase (EC 3.2.1.86) activity. These data suggest that SPy1599 is involved in the intracellular degradation of 6-phosphoglycosides, which are likely to originate from import through one of the organism's many phosphoenolpyruvate phosphotransfer systems (PEP-PTSs).

sted, utgiver, år, opplag, sider
2013. Vol. 69, s. 16-23
Emneord [en]
Glycosyl Hydrolases, Lactococcus-Lactis, Molecular-Graphics, Crystal-Structures, Diffraction Data, Binding, Protein, 6-Phospho-Beta-Galactosidase, Mechanism, Virulence
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-117639DOI: 10.1107/S0907444912041005ISI: 000312866500004Scopus ID: 2-s2.0-84871898138OAI: oai:DiVA.org:kth-117639DiVA, id: diva2:602553
Forskningsfinansiär
Formas
Merknad

QC 20130201

Tilgjengelig fra: 2013-02-01 Laget: 2013-02-01 Sist oppdatert: 2017-12-06bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstScopus

Søk i DiVA

Av forfatter/redaktør
Eklöf, Jens M.Thongpoo, PreeyanuchBrumer, Harry
Av organisasjonen
I samme tidsskrift
Acta Crystallographica Section D: Biological Crystallography

Søk utenfor DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric

doi
urn-nbn
Totalt: 76 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • 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