Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (Psr
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ARTICLE
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 Tim Schulte1 · Benedetta Maria Sala1,2 · Johan Nilvebrant2 · Per‑Åke Nygren2 · Adnane Achour1 · Andrey Shernyukov3,4 · Tatiana Agback3 · Peter Agback3 Received: 17 January 2020 / Accepted: 8 April 2020 © The Author(s) 2020
Abstract 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. Keywords NMR assignments · Pneumococcal serine rich repeat protein · Secondary structure · X-ray comparison · Backbone dynamics Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12104-020-09944-9) contains supplementary material, which is available to authorized users. * Peter Agback [email protected] 1
Science for Life Laboratory, Department of Medicine, Solna, Karolinska Institute, and Division of Infectious Diseases, Karolinska University Hospital, SE‑171 76 Stockholm, Sweden
2
Division of Protein Engineering, Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, AlbaNova University Center, Royal Institute of Technology, and Science for Life Laboratory, SE‑100 44 Stockholm, Sweden
3
Department of Molecular Sciences, Swedish University of Agricultural Sciences, PO Box 7015, 750 07 Uppsala, Sweden
4
Laboratory of Magnetic Radiospectroscopy, N.N. Vorozhtsov Institute of Organic Chemistry, SB RAS, Lavrentiev ave. 9, Novosibirsk, Russia 630090
Biological context The Gram-positive commensal and human-adapted bacterium Streptococcus pneumoniae colonizes the upper respiratory tract in about 10% of healthy adu
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