Purification, crystallization and preliminary crystallographic analysis of WsaF, an essential rhamnosyltransferase from Geobacillus stearothermophilus

Kerstin Steiner, Anna Wojciechowska, Christina Schaeffer, James H. Naismith

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

The beta 1,2-rhamnosyltransferase WsaF is involved in the biosynthesis of a polyrhamnan chain which is attached to the surface-layer protein from Geobacillus stearothermophilus NRS 2004/3a. The enzyme belongs to the large retaining GT4 family. To date, no structure of a rhamnosyltransferase has been published. Recombinant purified native WsaF has been crystallized, resulting in crystals that belonged to space group P2(1)2(1)2(1) with unit-cell parameters a = 50.5, b = 56.1, c = 276.8 angstrom and diffracted to 3.0 angstrom resolution. Selenomethionine-variant WsaF crystallized in space group P2(1) with unit-cell parameters a = 75.9, b = 75.5, c = 78.1 angstrom and diffracted to 2.3 angstrom resolution.

Original languageEnglish
Pages (from-to)1163-1165
Number of pages3
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume64
Issue number12
DOIs
Publication statusPublished - Dec 2008

Keywords

  • S-LAYER GLYCOPROTEIN
  • NRS 2004/3A
  • FAMILY GT4
  • GLYCOSYLTRANSFERASES
  • GLYCOSYLATION
  • BIOSYNTHESIS
  • CATALYSIS
  • INSIGHTS

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