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

Ana C Pereira; Ana Paiva; Ivo H Saraiva; Teresa Costa; Adriano O Henriques; Manolis Matzapetakis

doi:10.1007/s12104-014-9593-8

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

Biomol NMR Assign. 2015 Oct;9(2):285-8. doi: 10.1007/s12104-014-9593-8. Epub 2014 Dec 11.

Authors

Ana C Pereira¹, Ana Paiva¹, Ivo H Saraiva¹, Teresa Costa¹, Adriano O Henriques¹, Manolis Matzapetakis²

Affiliations

¹ Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal.
² Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157, Oeiras, Portugal. [email protected].

PMID: 25503291
DOI: 10.1007/s12104-014-9593-8

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.

Keywords: Bacillus subtilis; Cell wall; RodZ.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillus subtilis / metabolism*
Bacterial Proteins / chemistry*
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Secondary
Protein Structure, Tertiary
Proton Magnetic Resonance Spectroscopy

Substances

Bacterial Proteins