RT Journal Article
T1 Inter-hairpin linker sequences determine the structure of the ββ-solenoid fold: a “bottom-up” study of pneumococcal LytA choline-binding module.
A1 Maestro García-Donas, María Beatriz
A1 Zamora-Carreras, Hector
A1 Jiménez, Maria Angeles
A1 Sanz, Jesús
AB The ββ-solenoid structures are part of many proteins involved in the recognition of bacterial cell wall. They are elongated polypeptides consisting of repeated β-hairpins connected by linker sequences and disposed around a superhelical axis stabilised by short-range interactions. Among the most studied ββ-solenoids are those belonging to the family of choline-binding modules (CBMs) from the respiratory pathogen Streptococcus pneumoniae (pneumococcus) and its bacteriophages, and their properties have been employed to develop several biotechnological and biomedical tools. We have carried out a theoretical, spectroscopic and thermodynamic study of the ββ-solenoid structure of the CBM from the pneumococcal LytA autolysin using peptides of increasing length containing 1–3 repeats of this structure. Our results show that hints of native-like tertiary structure are only observed with a minimum of three β-hairpins, corresponding to one turn of the solenoid superhelix, and identify the linker sequences between hairpins as the major directors of the solenoid folding. This study paves the way for the rational structural engineering of ββ-solenoids aimed to find novel applications.
SN 0141-8130
YR 2021
FD 2021
LK https://hdl.handle.net/20.500.14352/94089.2
UL https://hdl.handle.net/20.500.14352/94089.2
LA eng
NO Maestro, Beatriz, et al. «Inter-Hairpin Linker Sequences Determine the Structure of the Ββ-Solenoid Fold: A “Bottom-up” Study of Pneumococcal LytA Choline-Binding Module». International Journal of Biological Macromolecules, vol. 190, noviembre de 2021, pp. 679-92. https://doi.org/10.1016/j.ijbiomac.2021.08.223.
NO European Commission
NO Ministerio de Ciencia, Innovación y Universidades (España)
NO Consejo Superior de Investigaciones Científicas
NO Instituto de Salud Carlos III
DS Docta Complutense
RD 10 abr 2025