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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, T. (author)
Karolinska Institutet
Sala, Benedetta Maria (author)
KTH,Proteinvetenskap
Nilvebrant, Johan, 1982- (author)
KTH,Albanova VinnExcellence Center for Protein Technology, ProNova
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Nygren, Per-Åke, 1961- (author)
KTH,Albanova VinnExcellence Center for Protein Technology, ProNova
Achour, A. (author)
Karolinska Institutet
Shernyukov, A. (author)
Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences,Vorozhtsov Novosibirsk Institute of Organic Chemistry
Agback, T. (author)
Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
Agback, Peter (author)
Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences
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 (creator_code:org_t)
 
2020-04-20
2020
English.
In: Biomolecular NMR Assignments. - : Springer. - 1874-2718 .- 1874-270X.
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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. 

Subject headings

NATURVETENSKAP  -- Biologi -- Strukturbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Structural Biology (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)

Keyword

Backbone dynamics
NMR assignments
Pneumococcal serine rich repeat protein
Secondary structure
X-ray comparison

Publication and Content Type

ref (subject category)
art (subject category)

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