6JHK

Crystal Structure of Bacillus subtilis RsbS

Summary for 6JHK

• Entry DOI: 10.2210/pdb6jhk/pdb
• Descriptor: RsbS negative regulator of sigma-B (1 entity in total)
• Functional Keywords: rsbs, stressosome, icosahedron, stas domain, protein binding
• Biological source: Bacillus subtilis
• Total number of polymer chains: 5
• Total formula weight: 67723.19

Authors

Kwon, E.,Pathak, D.,Dahal, P.,Kim, D.Y. (deposition date: 2019-02-18, release date: 2019-09-11, Last modification date: 2024-11-20)

Primary citation

Kwon, E.,Pathak, D.,Kim, H.U.,Dahal, P.,Ha, S.C.,Lee, S.S.,Jeong, H.,Jeoung, D.,Chang, H.W.,Jung, H.S.,Kim, D.Y.
Structural insights into stressosome assembly.
Iucrj, 6:938-947, 2019

PubMed Abstract: The stressosome transduces environmental stress signals to SigB to upregulate SigB-dependent transcription, which is required for bacterial viability. The stressosome core is composed of RsbS and at least one of the RsbR paralogs. A previous cryo-electron microscopy (cryo-EM) structure of the RsbRA-RsbS complex determined under a 2 symmetry restraint showed that the stressosome core forms a pseudo-icosahedron consisting of 60 STAS domains of RsbRA and RsbS. However, it is still unclear how RsbS and one of the RsbR paralogs assemble into the stressosome. Here, an assembly model of the stressosome is presented based on the crystal structure of the RsbS icosahedron and cryo-EM structures of the RsbRA-RsbS complex determined under diverse symmetry restraints (nonsymmetric 1, dihedral 2 and icosahedral envelopes). 60 monomers of the crystal structure of RsbS fitted well into the -restrained cryo-EM structure determined at 4.1 Å resolution, even though the STAS domains in the envelope were averaged. This indicates that RsbS and RsbRA share a highly conserved STAS fold. 22 protrusions observed in the 1 envelope, corresponding to dimers of the RsbRA N-domain, allowed the STAS domains of RsbRA and RsbS to be distinguished in the stressosome core. Based on these, the model of the stressosome core was reconstructed. The mutation of RsbRA residues at the binding interface in the model (R189A/Q191A) significantly reduced the interaction between RsbRA and RsbS. These results suggest that nonconserved residues in the conserved STAS folds between RsbS and RsbR paralogs determine stressosome assembly.

PubMed: 31576226
DOI: 10.1107/S205225251900945X

Experimental method

X-RAY DIFFRACTION (3.101 Å)