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 language | English (US) |
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Pages (from-to) | 520-523 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 69 |
Issue number | 5 |
DOIs | |
State | Published - May 2013 |
Externally published | Yes |
Keywords
- DUF1792
- Streptococcus parasanguinis
- glycosyltransferase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics