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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

Schulte, Tim and Sala, Benedetta Maria and Nilvebrant, Johan and Nygren, Per-Ake and Achour, Adnane and Sherniukov, Andrei and Agback, Tatiana and Agback, Peter (2020). 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. Biomolecular NMR Assignments. 14 , 195-200
[Journal article]

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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 beta-sheet on one side, and another beta-sheet that is distorted by loops and beta-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 beta-sheet formed between edge strands of two symmetry-related molecules, which could promote bacterial aggregation during biofilm formation. Here we report the near complete N-15/C-13/H-1 backbone resonance assignment of the BR domain of PsrP, revealing a secondary structure profile that is almost identical to the X-ray structure. Dynamic N-15-T-1, T-2 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.

Authors/Creators:Schulte, Tim and Sala, Benedetta Maria and Nilvebrant, Johan and Nygren, Per-Ake and Achour, Adnane and Sherniukov, Andrei and Agback, Tatiana and Agback, Peter
Title: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
Year of publishing :2020
Volume:14
Page range:195-200
Number of Pages:6
ISSN:1874-2718
Language:English
Publication Type:Journal article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 3 Medical and Health Sciences > 301 Basic Medicine > Cell and Molecular Biology
Keywords:NMR assignments, Pneumococcal serine rich repeat protein, Secondary structure, X-ray comparison, Backbone dynamics
URN:NBN:urn:nbn:se:slu:epsilon-p-105419
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-105419
Additional ID:
Type of IDID
DOI10.1007/s12104-020-09944-9
Web of Science (WoS)000527445300001
ID Code:17792
Faculty:NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(NL, NJ) > Department of Molecular Sciences
Deposited By: SLUpub Connector
Deposited On:13 Oct 2020 10:45
Metadata Last Modified:13 Oct 2020 11:18

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