RT Journal Article
T1 Structural autonomy of a beta-hairpin peptide derived from the pneumococcal choline-binding protein LytA
A1 Maestro García-Donas, María Beatriz
A1 Santiveri, C. M.
A1 Jimenez, M. A.
A1 Sanz, J. M.
AB The 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.
PB Oxford University Press
SN 1741-0126
YR 2010
FD 2010-11-04
LK https://hdl.handle.net/20.500.14352/93162
UL https://hdl.handle.net/20.500.14352/93162
LA eng
NO Ministerio de Ciencia e Innovación (MICIN)
NO Comisión Europea
DS Docta Complutense
RD 6 abr 2025