Open AccessExpression, crystallization and preliminary X‐ray analysis of the periplasmic stress sensory protein RseB from Escherichia coli
Author(s) -
Zeth Kornelius,
Wollmann Petra
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106027825
Subject(s) - periplasmic space , escherichia coli , crystallization , stress (linguistics) , x ray , crystallography , materials science , chemistry , biochemistry , physics , gene , optics , organic chemistry , linguistics , philosophy
Sensing external stress in the bacterial periplasm and signal transduction to the cytoplasm are important functions of the CpxAR, Bae and σ E signalling pathways. In Escherichia coli , the σ E pathway can be activated through degradation of the antisigma factor RseA by DegS and YaeL. The periplasmic protein RseB plays an important role in this pathway by exerting a direct or indirect negative effect on YaeL cleavage efficiency. RseB from E. coli , missing the periplasmic signal sequence (RseB ΔN ), was cloned, expressed, purified and crystallized. Crystals were obtained in two different forms belonging to space group P 42 1 2 (form I) and C 222 1 (form II) and diffracted to 2.8 and 2.4 Å resolution, respectively. In crystal form I two copies of the protein were located in the asymmetric unit according to heavy‐atom analysis, while crystal form II contained three copies.