view article
Figure 1
The structure of the RsbS monomer. (a) Sequence alignment of STAS proteins. The sequences of B. subtilis (Bs) RsbS, M. thermoacetica (Mt) RsbS and Bs RsbR proteins (RsbRA, RsbRB, RsbRC and RsbRD) were aligned. Identical and homologous residues are boxed in red and yellow, respectively. The secondary structure of Bs RsbS is displayed using cylinders for α-helices and arrows for β-strands. The phosphorylation sites on RsbS and RsbR, which are crucial for the regulation of SigB activation signaling, are marked with blue and red triangles, respectively. (b) The structure of the RsbS monomer. The ribbon models are shown in two different orientations. α-Helices, β-strands and loops are colored red, yellow and green, respectively. The secondary structures are labeled using the same scheme as in (a). The phosphorylated Ser59 is shown as a stick model. (c) Structural comparison of STAS proteins. The structures of mtSTAS (PDB entry 3ztb; Quin et al., 2012BB60) and gsSpoIIAB (PDB entry 1til; Masuda et al., 2004BB61) were superimposed onto RsbS. Cα trace models were drawn in the same orientation as in the left panel of (b). Red, green and blue represent RsbS, mtSTAS and gsSpoIIAB, respectively.

IUCrJ
Volume 6| Part 5| September 2019| Pages 938-947
ISSN: 2052-2525
https://doi.org/10.1107/S205225251900945X