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

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 Научная публикация

Журнал

Biomolecular NMR Assignments
ISSN: 1874-2718 , E-ISSN: 1874-270X

Вых. Данные

Год: 2020, DOI: 10.1007/s12104-020-09944-9

Ключевые слова

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

Авторы

Schulte Tim ^1,2 , Sala Benedetta Maria ^1,2,3,4 , Nilvebrant Johan ^3,4 , Nygren Per-Ake ^3,4 , Achour Adnane ^1,2 , Shernyukov Andrey ^5,6 , Agback Tatiana ⁵ , Agback Peter ⁵

Организации

1	(Данные Web of science) Karolinska Univ Hosp, Karolinska Inst, Dept Med, Sci Life Lab, SE-17176 Stockholm, Sweden
2	(Данные Web of science) Karolinska Univ Hosp, Div Infect Dis, SE-17176 Stockholm, Sweden
3	(Данные Web of science) AlbaNova Univ Ctr, Royal Inst Technol, Sch Engn Sci Chem Biotechnol & Hlth, Dept Prot Sci,Div Prot Engn, SE-10044 Stockholm, Sweden
4	(Данные Web of science) Sci Life Lab, SE-10044 Stockholm, Sweden
5	(Данные Web of science) Swedish Univ Agr Sci, Dept Mol Sci, POB 7015, S-75007 Uppsala, Sweden
6	(Данные Web of science) RAS, NN Vorozhtsov Inst Organ Chem, Lab Magnet Radiospectroscopy, SB, Lavrentiev Ave 9, Novosibirsk 630090, Russia

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.

Schulte T. , Sala B.M. , Nilvebrant J. , Nygren P-A. , Achour A. , Shernyukov A. , Agback T. , Agback P.
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. 2020. DOI: 10.1007/s12104-020-09944-9 WOS Scopus

Полный текст от издателя

Опубликована online:	20 апр. 2020 г.
Опубликована в печати:	1 окт. 2020 г.

Web of science	WOS:000527445300001
Scopus	2-s2.0-85084065293
OpenAlex	W3016766706