Preliminary X‐ray crystallographic studies of an N‐terminal domain of unknown function from a putative glycosyltransferase from Streptococcus parasanguinis. Issue 5 (22nd May 2013)

• Record Type: Journal Article
• Authors: Zhang, Hua; Zhu, Fan; Ding, Lei; Zhou, Meixian; Wu, Ren; Wu, Hui
• Is Part Of: Acta crystallographica. Volume 69:Issue 5(2013:May)
• Page Start: 520
• Page End: 523
• Publication Date: 2013-05-22
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113007161
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Streptococcus parasanguinis</italic> 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 <italic>C</italic>2, with unit‐cell parameters <italic>a</italic> = 71.0, <italic>b</italic> = 45.1, <italic>c</italic> = 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%.</p> </abstract>