Unknown

Dataset Information

0

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


ABSTRACT: The beta1,2-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 A and diffracted to 3.0 A resolution. Selenomethionine-variant WsaF crystallized in space group P2(1) with unit-cell parameters a = 75.9, b = 75.5, c = 78.1 A and diffracted to 2.3 A resolution.

SUBMITTER: Steiner K 

PROVIDER: S-EPMC2593710 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Steiner Kerstin K   Wojciechowska Anna A   Schäffer Christina C   Naismith James H JH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20081128 Pt 12


The beta1,2-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 A and diffra  ...[more]

Similar Datasets

| S-EPMC3936444 | biostudies-literature
| S-EPMC3614171 | biostudies-literature
| S-EPMC3792669 | biostudies-literature
| S-EPMC3668598 | biostudies-literature
| S-EPMC1978154 | biostudies-literature
| S-EPMC2593709 | biostudies-literature
| S-EPMC4259239 | biostudies-literature
| S-EPMC2330136 | biostudies-literature
| S-EPMC5012207 | biostudies-literature
| S-EPMC3144798 | biostudies-literature