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Structure paper

TitleActivation mechanism of the full-length histidine kinase LvrB from pathogenic Leptospira.
Journal, issue, pagesNat Commun, Vol. 17, Year 2026
Publish dateDec 13, 2023 (structure data deposition date)
AuthorsAgustoni, E. / Mechaly, A. / Dalla Rizza, J. / Beriashvili, D. / Pluhackova, K. / Isaikina, P. / Trajtenberg, F. / Muntener, T. / Wunder Jr., E.A. / Ko, A.I. ...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.
External linksNat Commun / PubMed:41991510
MethodsX-ray diffraction
Resolution2.65 Å
Structure data

PDB-8vc9:
Crystal structure of Rec-controlled histidine kinase LvrB, BeF3-activated
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-ACP:
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / AMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • leptospira interrogans serovar copenhageni (bacteria)
KeywordsSIGNALING PROTEIN / two component systems / hybrid response regulator / seudo-phosphorylated form

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