6COO

CSP1-E1A

Summary for 6COO

• Entry DOI: 10.2210/pdb6coo/pdb
• NMR Information: BMRB: 30427
• Descriptor: Competence-stimulating peptide type 1 (1 entity in total)
• Functional Keywords: pneumococcus, quorum sensing, signaling molecule, csp, signaling protein
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 2190.70

Authors

Yang, Y. (deposition date: 2018-03-12, release date: 2018-08-29, Last modification date: 2024-05-01)

Primary citation

Yang, Y.,Cornilescu, G.,Tal-Gan, Y.
Structural Characterization of Competence-Stimulating Peptide Analogues Reveals Key Features for ComD1 and ComD2 Receptor Binding in Streptococcus pneumoniae.
Biochemistry, 57:5359-5369, 2018

PubMed Abstract: Streptococcus pneumoniae is an important pathogen that utilizes quorum sensing (QS) to regulate genetic transformation, virulence, and biofilm formation. The competence-stimulating peptide (CSP) is a 17-amino acid signal peptide that is used by S. pneumoniae to trigger QS. S. pneumoniae strains can be divided into two main specificity groups based on the CSP signal they produce (CSP1 or CSP2) and their compatible receptors (ComD1 or ComD2, respectively). Modulation of QS in S. pneumoniae can be achieved by targeting the CSP:ComD interaction using synthetic CSP analogues. However, to rationally design CSP-based QS modulators with enhanced activities, an in-depth understanding of the structural features that are required for receptor binding is needed. Herein, we report a comprehensive in-solution three-dimensional structural characterization of eight CSP1 and CSP2 analogues with varied biological activities using nuclear magnetic resonance spectroscopy. Analysis of these structures revealed two distinct hydrophobic patches required for effective ComD1 and ComD2 binding.

PubMed: 30125091
DOI: 10.1021/acs.biochem.8b00653

Experimental method

SOLUTION NMR