Preliminary X-ray crystallographic studies of an N-terminal domain of unknown function from a putative glycosyltransferase from Streptococcus parasanguinis

Hua Zhang, Fan Zhu, Lei Ding, Meixian Zhou, Ren Wu, Hui Wu

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Serine-rich repeat glycoproteins (SRRPs) belong to a growing family of bacterial adhesins; they play important roles in bacterial virulence. Fap1, the first SRRP protein to be identified, is glycosylated; while the first two steps of its glycosylation have been determined, the remaining glycosylation steps are unknown. In a search for proteins that might be relevant to the glycosylation of Fap1, a putative glycosyltransferase (GalT1) from Streptococcus parasanguinis was identified. GalT1 possesses a domain of unknown function at the N-terminus. This domain is highly conserved in bacteria and is a member of a broad superfamily. However, the structure of this domain has not been determined. Here, the conditions used to produce a recombinant version of this protein domain and to grow protein crystals are reported. The crystals obtained belonged to space group C2, with unit-cell parameters a = 71.0, b = 45.1, c = 78.6 Å, β = 109.6°, and diffracted to 1.55 Å resolution at a synchrotron X-ray source. This domain does not share sequence identity with proteins of known structures above a level of 12%.

Original languageEnglish (US)
Pages (from-to)520-523
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number5
DOIs
StatePublished - May 2013
Externally publishedYes

Keywords

  • DUF1792
  • glycosyltransferase
  • Streptococcus parasanguinis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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