A model for the full-length structure of the blue light-sensing protein YtvA from Bacillus subtilis has been determined by EPR spectroscopy, performed on spin labels selectively inserted at amino acid positions 54, 80, 117 and 179. Our data indicate that YtvA forms a dimer in solution and enable us, based on the known structures of the individual domains and modelling, to propose a three-dimensional model for the full length protein. Most importantly, this includes the YtvA N-terminus that has so far not been identified in any structural model. We show that our data are in agreement with the crystal structure of an engineered LOV-domain protein, YF1, that shows the N-terminus of the protein to be helical and to fold back in between the β-sheets of the two LOV domains, and argue for an identical arrangement in YtvA. While we could not detect any structural changes upon blue-light activation of the protein, this structural model now forms an ideal basis for identifying residues as targets for further spin labelling studies to detect potential conformational changes upon irradiation of the protein.
A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis, based on EPR spectroscopy / Christopher, Engelhard; Sarah, Raffelberg; Yifen, Tang; Ralph P., Diensthuber; Andreas, Möglich; Losi, Aba; Wolfgang, Gärtner; Robert, Bittl. - In: PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES. - ISSN 1474-905X. - 12:(2013), pp. 1855-1863. [10.1039/c3pp50128k]
A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis, based on EPR spectroscopy
LOSI, Aba;
2013-01-01
Abstract
A model for the full-length structure of the blue light-sensing protein YtvA from Bacillus subtilis has been determined by EPR spectroscopy, performed on spin labels selectively inserted at amino acid positions 54, 80, 117 and 179. Our data indicate that YtvA forms a dimer in solution and enable us, based on the known structures of the individual domains and modelling, to propose a three-dimensional model for the full length protein. Most importantly, this includes the YtvA N-terminus that has so far not been identified in any structural model. We show that our data are in agreement with the crystal structure of an engineered LOV-domain protein, YF1, that shows the N-terminus of the protein to be helical and to fold back in between the β-sheets of the two LOV domains, and argue for an identical arrangement in YtvA. While we could not detect any structural changes upon blue-light activation of the protein, this structural model now forms an ideal basis for identifying residues as targets for further spin labelling studies to detect potential conformational changes upon irradiation of the protein.File | Dimensione | Formato | |
---|---|---|---|
c3pp50128k (1).pdf
non disponibili
Tipologia:
Documento in Post-print
Licenza:
NON PUBBLICO - Accesso privato/ristretto
Dimensione
1.52 MB
Formato
Adobe PDF
|
1.52 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.