Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-alpha-arabinanase from Bacillus subtilis.
Two Bacillus subtilis extracellular endo-1,5-alpha-L-arabinanases, AbnA and Abn2, belonging to glycoside hydrolase family 43 have been identified. The recently characterized Abn2 protein hydrolyzes arabinan and has low identity to other reported 1,5-alpha-L-arabinanases. Abn2 and its selenomethionine (SeMet) derivative have been purified and crystallized. Crystals appeared in two different space groups: P1, with unit-cell parameters a = 51.9, b = 57.6, c = 86.2 A, alpha = 82.3, beta = 87.9, gamma = 63.6 degrees , and P2(1)2(1)2(1), with unit-cell parameters a = 57.9, b = 163.3, c = 202.0 A. X-ray data have been collected for the native and the SeMet derivative to 1.9 and 2.7 A resolution, respectively. An initial model of Abn2 is being built in the SeMet-phased map.
de Sanctis
Daniele
D
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República-EAN, 2780-157 Oeiras, Portugal. desanctisd@gmail.com
Bento
Isabel
I
Inácio
José Manuel
JM
Custódio
Sónia
S
de Sá-Nogueira
Isabel
I
Carrondo
Maria Arménia
MA
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D003460:Crystallization; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D006026:Glycoside Hydrolases; C082526:arabinan endo-1,5-alpha-L-arabinosidase