The SecB-like chaperone Rv1957 from Mycobacterium tuberculosis: crystallization and X-ray crystallographic analysis

Autor: Han Wang, Zuokun Lu, TingTing Yu
Rok vydání: 2016
Předmět:
Zdroj: Acta crystallographica. Section F, Structural biology communications. 72(Pt 6)
ISSN: 2053-230X
Popis: Protein export is important in all bacteria, and bacteria have evolved specialized export machineries to fulfil this task. InMycobacterium tuberculosis, the causative agent of tuberculosis, the general secretion pathway (Sec pathway) is conserved and is essential in performing the export of proteins. The bacterial Sec pathway post-translationally exports unfolded proteins out of the cytoplasm, and the core of the Sec pathway is composed of a heterotrimeric membrane-embedded channel, SecYEG, and two cytosolic components, SecA and SecB. SecB functions by stabilizing unfolded proteins, maintaining them in an export-competent state. Although SecB is mainly found in Proteobacteria, a SecB-like protein, Rv1957, that controls a stress-response toxin–antitoxin system, is found inM. tuberculosis. Rv1957 can also functionally replace theEscherichia coliSecB chaperone bothin vivoandin vitro. In this work, the production, crystallization and X-ray crystallographic analysis of Rv1957 are reported. Notably, diffraction-quality crystals were obtained only at high concentrations of dimethyl sulfoxide,i.e.about 12%(v/v). The crystals of Rv1957 belonged to space groupP212121, with unit-cell parametersa= 64.5,b= 92.0,c= 115.4 Å.
Databáze: OpenAIRE