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 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
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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. |
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ISSN: | 1874-2718 1874-270X |
DOI: | 10.1007/s12104-014-9593-8 |