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Structural basis fo...
Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria
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- Hall, Michael (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Grundström, Christin (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Begum, Afshan (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Lindberg, Mikael J. (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Sauer, Uwe H. (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Almqvist, Fredrik (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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- Johansson, Jörgen (författare)
- Umeå universitet,Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten),Molekylär Infektionsmedicin, Sverige (MIMS)
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- Sauer-Eriksson, A. Elisabeth (författare)
- Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR)
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(creator_code:org_t)
- 2016-12-05
- 2016
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 113:51, s. 14733-14738
- Relaterad länk:
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https://doi.org/10.1...
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https://www.pnas.org...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfAWT in complex only with DNA confirms that PrfAWT can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction.
Ämnesord
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Medicinsk genetik (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medical Genetics (hsv//eng)
Nyckelord
- Listeria
- PrfA
- activation
- glutathione
- virulence
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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