XACb0070 is an uncharacterized protein coded by the two large plasmids isolated from Xanthomonas axonopodis pv. citri, the agent of citrus canker and responsible for important economical losses in citrus world production. XACb0070 presents sequence homology only with other hypothetical proteins belonging to plant pathogens, none of which have their structure determined. The NMR-derived solution structure reveals this protein is a homodimer in which each monomer presents two domains with different structural and dynamic properties: a folded N-terminal domain with beta alpha alpha topology which mediates dimerization and a long disordered C-terminal tail. The folded domain shows high structural similarity to the ribbon-helix-helix transcriptional repressors, a family of DNA-binding proteins of conserved 3D fold but low sequence homology: indeed XACb0070 binds DNA. Primary sequence and fold comparison of XACb0070 with other proteins of the ribbon-helix-helix family together with examination of the genes in the vicinity of xacb0070 suggest the protein might be the component of a toxin-antitoxin system.

Gallo, M., Ferrari, E., Eliseo, T., Amata, I., Pertinhez, T., Katsuyama, A., et al. (2010). A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv.citri. JOURNAL OF STRUCTURAL BIOLOGY, 170(1), 21-31 [10.1016/j.jsb.2009.12.022].

A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv.citri

PACI, MAURIZIO;CICERO, DANIEL OSCAR
2010-04-01

Abstract

XACb0070 is an uncharacterized protein coded by the two large plasmids isolated from Xanthomonas axonopodis pv. citri, the agent of citrus canker and responsible for important economical losses in citrus world production. XACb0070 presents sequence homology only with other hypothetical proteins belonging to plant pathogens, none of which have their structure determined. The NMR-derived solution structure reveals this protein is a homodimer in which each monomer presents two domains with different structural and dynamic properties: a folded N-terminal domain with beta alpha alpha topology which mediates dimerization and a long disordered C-terminal tail. The folded domain shows high structural similarity to the ribbon-helix-helix transcriptional repressors, a family of DNA-binding proteins of conserved 3D fold but low sequence homology: indeed XACb0070 binds DNA. Primary sequence and fold comparison of XACb0070 with other proteins of the ribbon-helix-helix family together with examination of the genes in the vicinity of xacb0070 suggest the protein might be the component of a toxin-antitoxin system.
apr-2010
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Protein Conformation; Electrophoresis, Polyacrylamide Gel; Nuclear Magnetic Resonance, Biomolecular; Base Sequence; Plasmids; Dimerization; Models, Molecular; Xanthomonas axonopodis; Citrus; Sequence Analysis, DNA; Spectrometry, Fluorescence; Transcription Factors; Molecular Sequence Data; Amino Acid Sequence
Gallo, M., Ferrari, E., Eliseo, T., Amata, I., Pertinhez, T., Katsuyama, A., et al. (2010). A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv.citri. JOURNAL OF STRUCTURAL BIOLOGY, 170(1), 21-31 [10.1016/j.jsb.2009.12.022].
Gallo, M; Ferrari, E; Eliseo, T; Amata, I; Pertinhez, T; Katsuyama, A; Paci, M; Farah, C; Spisni, A; Cicero, Do
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/13127
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