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

Authors :
Pereira AC
Paiva A
Saraiva IH
Costa T
Henriques AO
Matzapetakis M
Source :
Biomolecular NMR assignments [Biomol NMR Assign] 2015 Oct; Vol. 9 (2), pp. 285-8. Date of Electronic Publication: 2014 Dec 11.
Publication Year :
2015

Abstract

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.

Details

Language :
English
ISSN :
1874-270X
Volume :
9
Issue :
2
Database :
MEDLINE
Journal :
Biomolecular NMR assignments
Publication Type :
Academic Journal
Accession number :
25503291
Full Text :
https://doi.org/10.1007/s12104-014-9593-8