PDBsum entry 6t3h

Transcription

PDB id: 6t3h

Contents

Protein chains

357 a.a.

PDB id:

6t3h

Name:

Transcription

Title:

Structure of the rap conjugation gene regulator of the plasmid pls20 in apo form

Structure:

Response regulator aspartate phosphatase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Bacillus subtilis subsp. Natto. Organism_taxid: 86029. Gene: rapa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

3.04Å R-factor: 0.204 R-free: 0.259

Authors:

I.Crespo,N.Bernardo,W.J.J.Meijer,D.R.Boer

Key ref:

I.Crespo et al. (2020). Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization. Nucleic Acids Res, 48, 8113-8127. PubMed id: 32658272 DOI: 10.1093/nar/gkaa540

Date:

11-Oct-19 Release date: 24-Jun-20

Protein chains

E9RIY6  (E9RIY6_BACNA) -  Response regulator aspartate phosphatase from Bacillus subtilis subsp. natto

Seq: 368 a.a.

Struc: 357 a.a.

DOI no: 10.1093/nar/gkaa540

Nucleic Acids Res 48:8113-8127 (2020)

PubMed id: 32658272

Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization.

I.Crespo, N.Bernardo, A.Miguel-Arribas, P.K.Singh, J.R.Luque-Ortega, C.Alfonso, M.Malfois, W.J.J.Meijer, D.R.Boer.

ABSTRACT

Quorum sensing allows bacterial cells to communicate through the release of soluble signaling molecules into the surrounding medium. It plays a pivotal role in controlling bacterial conjugation in Gram-positive cells, a process that has tremendous impact on health. Intracellular regulatory proteins of the RRNPP family are common targets of these signaling molecules. The RRNPP family of gene regulators bind signaling molecules at their C-terminal domain (CTD), but have highly divergent functionalities at their N-terminal effector domains (NTD). This divergence is also reflected in the functional states of the proteins, and is highly interesting from an evolutionary perspective. RappLS20 is an RRNPP encoded on the Bacillus subtilis plasmid pLS20. It relieves the gene repression effectuated by RcopLS20 in the absence of the mature pLS20 signaling peptide Phr*pLS20. We report here an in-depth structural study of apo and Phr*pLS20-bound states of RappLS20 at various levels of atomic detail. We show that apo-RappLS20 is dimeric and that Phr*pLS20-bound Rap forms NTD-mediated tetramers. In addition, we show that RappLS20 binds RcopLS20 directly in the absence of Phr*pLS20 and that addition of Phr*pLS20 releases RcopLS20 from RappLS20. This allows RcopLS20 to bind the promotor region of crucial conjugation genes blocking their expression.