Chemical shift assignments and secondary structure determination of the ectodomain of Bacillus subtilis morphogenic protein RodZ

RodZ (also known as YfgA) is a component of the core bacterial morphogenic apparatus. RodZ is a key cell shape determinant in rod-shaped bacteria and it interacts with the actin-like cytoskeletal protein MreB. In Bacillus subtilis , this 304-residue transmembrane protein is composed of three distinc...

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Veröffentlicht in:Biomolecular NMR assignments 2015-10, Vol.9 (2), p.285-288
Hauptverfasser: Pereira, Ana C., Paiva, Ana, Saraiva, Ivo H., Costa, Teresa, Henriques, Adriano O., Matzapetakis, Manolis
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Sprache:eng
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Zusammenfassung:RodZ (also known as YfgA) is a component of the core bacterial morphogenic apparatus. RodZ is a key cell shape determinant in rod-shaped bacteria and it interacts with the actin-like cytoskeletal protein MreB. In Bacillus subtilis , this 304-residue transmembrane protein is composed of three distinct domains: a cytoplasmic domain (RodZn), a transmembrane domain, and an extra-cytoplasmic domain (RodZc). Here we report the 1 H, 13 C and 15 N backbone and side chain resonance assignments of the RodZc domain from B. subtilis by NMR spectroscopy, and the resulting secondary structure prediction.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-014-9593-8