Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution
Autor: | Tim Schulte, Per-Åke Nygren, Andrey Shernyukov, Johan Nilvebrant, Benedetta Maria Sala, Tatiana Agback, Adnane Achour, Peter Agback |
---|---|
Rok vydání: | 2020 |
Předmět: |
NMR assignments
Stereochemistry Proton Magnetic Resonance Spectroscopy Pneumococcal serine rich repeat protein Crystal structure Ligands Biochemistry Article Serine 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Protein Domains Structural Biology Secondary structure Molecule Carbon-13 Magnetic Resonance Spectroscopy Nuclear Magnetic Resonance Biomolecular Protein secondary structure 030304 developmental biology 0303 health sciences Nitrogen Isotopes 030306 microbiology Chemistry Biofilm Adhesion Backbone dynamics X-ray comparison Solutions Streptococcus pneumoniae Monomer Structural biology Cell and Molecular Biology |
Zdroj: | Biomolecular Nmr Assignments |
ISSN: | 1874-270X 1874-2718 |
Popis: | The pneumococcal serine rich repeat protein (PsrP) is displayed on the surface of Streptococcus pneumoniae with a suggested role in colonization in the human upper respiratory tract. Full-length PsrP is a 4000 residue-long multi-domain protein comprising a positively charged functional binding region (BR) domain for interaction with keratin and extracellular DNA during pneumococcal adhesion and biofilm formation, respectively. The previously determined crystal structure of the BR domain revealed a flat compressed barrel comprising two sides with an extended β-sheet on one side, and another β-sheet that is distorted by loops and β-turns on the other side. Crystallographic B-factors indicated a relatively high mobility of loop regions that were hypothesized to be important for binding. Furthermore, the crystal structure revealed an inter-molecular β-sheet formed between edge strands of two symmetry-related molecules, which could promote bacterial aggregation during biofilm formation. Here we report the near complete 15N/13C/1H backbone resonance assignment of the BR domain of PsrP, revealing a secondary structure profile that is almost identical to the X-ray structure. Dynamic 15N-T1, T2 and NOE data suggest a monomeric and rigid structure of BR with disordered residues only at the N- and C-termini. The presented peak assignment will allow us to identify BR residues that are crucial for ligand binding. |
Databáze: | OpenAIRE |
Externí odkaz: |