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TitleStructural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.
Journal, issue, pagesBiochem J, Vol. 473, Issue 14, Page 2239-2248, Year 2016
Publish dateJul 15, 2016
AuthorsHalina Wojtowicz / Ada Prochnicka-Chalufour / Gisele Cardoso de Amorim / Olga Roudenko / Catherine Simenel / Idir Malki / Gérard Pehau-Arnaudet / Francesca Gubellini / Alexandros Koutsioubas / Javier Pérez / Philippe Delepelaire / Muriel Delepierre / Rémi Fronzes / Nadia Izadi-Pruneyre /
PubMed AbstractBacteria use diverse signalling pathways to adapt gene expression to external stimuli. In Gram-negative bacteria, the binding of scarce nutrients to membrane transporters triggers a signalling ...Bacteria use diverse signalling pathways to adapt gene expression to external stimuli. In Gram-negative bacteria, the binding of scarce nutrients to membrane transporters triggers a signalling process that up-regulates the expression of genes of various functions, from uptake of nutrient to production of virulence factors. Although proteins involved in this process have been identified, signal transduction through this family of transporters is not well understood. In the present study, using an integrative approach (EM, SAXS, X-ray crystallography and NMR), we have studied the structure of the haem transporter HasR captured in two stages of the signalling process, i.e. before and after the arrival of signalling activators (haem and its carrier protein). We show for the first time that the HasR domain responsible for signal transfer: (i) is highly flexible in two stages of signalling; (ii) extends into the periplasm at approximately 70-90 Å (1 Å=0.1 nm) from the HasR β-barrel; and (iii) exhibits local conformational changes in response to the arrival of signalling activators. These features would favour the signal transfer from HasR to its cytoplasmic membrane partners.
External linksBiochem J / PubMed:27208170 / PubMed Central
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-3978:
EM map of HasR, a TonB dependent hemophore receptor from Serratia marcescens.
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-4187:
EM map of HasR, a TonB dependent receptor from Serratia marcescens in complex with the hemophore HasA and heme.
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Serratia marcescens (bacteria)

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