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Open AccessArticle

High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila

1
School of Life Science, Anhui University, Hefei 230601, Anhui, China
2
Institute of Physical Science and Information Technology, Anhui University, Hefei 230601, Anhui, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Crystals 2018, 8(2), 54; https://doi.org/10.3390/cryst8020054
Received: 25 November 2017 / Revised: 17 January 2018 / Accepted: 20 January 2018 / Published: 23 January 2018
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
Legionella pneumophila RpoS (LpRpoS), an alternative sigma factor of RNA polymerase (RNAP), is essential for virulence and stress resistance. To investigate the mechanism of RpoS in the intracellular pathogen L. pneumophila, we determined the high-resolution crystal structure of the LpRpoS 95–195 containing a partial region 1.2 and region 2. The structure of LpRpoS 95–195 reveals that the conserved residues are critical for promoter melting, DNA and core RNAP binding. The differences in regulatory factor binding site between Escherichia coli RpoS and LpRpoS suggest that LpRpoS may employ a distinct mechanism to recruit alternative regulatory factors controlling transcription initiation. View Full-Text
Keywords: RpoS; crystal structure; Legionella pneumophila; intracellular pathogen; regulatory factor RpoS; crystal structure; Legionella pneumophila; intracellular pathogen; regulatory factor
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MDPI and ACS Style

Zhang, N.; Chen, X.; Gong, X.; Li, T.; Xie, Z.; Hameed, M.F.; Wang, M.; Ge, H. High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila. Crystals 2018, 8, 54.

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