9QR2
EM structure of Rec-controlled histidine kinase LvrB
Summary for 9QR2
| Entry DOI | 10.2210/pdb9qr2/pdb |
| Related | 8VC9 9QQW |
| EMDB information | 53316 |
| Descriptor | histidine kinase, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | histidine kinase, signaling protein |
| Biological source | Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 |
| Total number of polymer chains | 2 |
| Total formula weight | 87948.24 |
| Authors | Agustino, E.,Buschiazzo, A.,Hiller, S.,Beriashvili, D. (deposition date: 2025-04-02, release date: 2026-04-15, Last modification date: 2026-10-07) |
| Primary citation | Agustoni, E.,Mechaly, A.,Dalla Rizza, J.,Beriashvili, D.,Pluhackova, K.,Isaikina, P.,Trajtenberg, F.,Muntener, T.,Wunder Jr., E.A.,Ko, A.I.,Schirmer, T.,Buschiazzo, A.,Hiller, S. Activation mechanism of the full-length histidine kinase LvrB from pathogenic Leptospira. Nat Commun, 17:-, 2026 Cited by PubMed Abstract: Pathogenic Leptospira modulate their virulence via the Lvr signaling system, with the histidine kinase LvrB being a central element. LvrB is a prototype of Rec-controlled histidine kinases, which are frequently found in bacterial two-component systems, and yet whose regulatory mechanisms remain largely unknown. Here, we report full-length structures of LvrB in different states uncovering its mechanism of activation. Kinase-inactive LvrB is a symmetric homodimer, with its catalytic domains rigidly clasped onto the central helical domain. Phosphorylation of the N-terminal Rec domains induces coiled-coil formation of the central αS helices thereby breaking symmetry through liberation of the catalytic domains into a dynamic, auto-phosphorylation competent state. We further identified LvrB's downstream effector partner LvrC, an anti-σ factor that reprograms the transcription of hundreds of virulence genes. Our findings set a mechanistic paradigm for Rec-controlled histidine kinases enabling the design of virulence inhibitors. PubMed: 41991510DOI: 10.1038/s41467-026-71783-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.24 Å) |
Structure validation
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