Maestro García-Donas, María BeatrizSantiveri, ClaraJimenez, María AngelesSanz, Jesús2024-01-232024-01-152024-01-232010Beatriz Maestro, Clara M. Santiveri, M. Angeles Jiménez, Jesús M. Sanz, Structural autonomy of a β-hairpin peptide derived from the pneumococcal choline-binding protein LytA, Protein Engineering, Design and Selection, Volume 24, Issue 1-2, January-February 2011, Pages 113–122, https://doi.org/10.1093/protein/gzq0871741-012610.1093/protein/gzq087https://hdl.handle.net/20.500.14352/93162.2The cell wall of Streptococcus pneumoniae and several other micro-organisms is decorated with a number of the so-called choline-binding proteins (CBPs) that recognise the choline residues in the bacterial surface by means of highly conserved, concatenated 20-aa sequences termed choline-binding repeats (CBRs), that are composed of a loop and a β-hairpin structure. In this work, we have investigated the ability to fold in aqueous solution of a 14-aa peptide (LytA197–210[wt]) and a single derivative of it, LytA197–210[ND], corresponding to one of the six β-hairpins of the LytA pneumococcal amidase. Intrinsic fluorescence and circular dichroism spectroscopical measurements showed that both peptides spontaneously acquire a non-random conformation which is also able to bind the natural ligand choline. Furthermore, nuclear magnetic resonance techniques allowed the calculation of the structure of the LytA197–210[ND] peptide, which displayed a β-hairpin conformation highly similar to that found within the full-length C-LytA module. These results provide a structural basis for the modular organisation of CBPs and suggest the use of CBRs as new templates for the design of stable β-hairpins.engAttribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/journal article1741-0134https://doi.org/10.1093/protein/gzq087open access577.1Choline-binding repeatsMosaic proteinsNMRPeptide structureStreptococcus pneumoniaeBioquímica (Química)2403 Bioquímica