Open AccessExpression, crystallization and preliminary crystallographic study of GluB from Corynebacterium glutamicum
Author(s) -
Liu Qingbo,
Li Defeng,
Hu Yonglin,
Wang DaCheng
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113011652
Subject(s) - corynebacterium glutamicum , glutamic acid , corynebacterium , biochemistry , crystallization , amino acid , bacteria , chemistry , substrate (aquarium) , transmembrane protein , biology , gene , organic chemistry , ecology , genetics , receptor
GluB is a substrate‐binding protein (SBP) which participates in the uptake of glutamic acid in Corynebacterium glutamicum , a Gram‐positive bacterium. It is part of an ATP‐binding cassette (ABC) transporter system. Together with the transmembrane proteins GluC and GluD and the cytoplasmic protein GluA, which couples the hydrolysis of ATP to the translocation of glutamate, they form a highly active glutamate‐uptake system. As part of efforts to study the amino‐acid metabolism, especially the metabolism of glutamic acid by C. glutamicum , a bacterium that is widely used in the industrial production of glutamic acid, the GluB protein was expressed, purified and crystallized, an X‐ray diffraction data set was collected to a resolution of 1.9 Å and preliminary crystallographic analysis was performed. The crystal belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 82.50, c = 72.69 Å.