Crystallographic and NMR Study of <i>Streptococcus pneumonia</i> LCP Protein Psr<sub>Sp</sub> Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity

Crystallographic and NMR Study of <i>Streptococcus pneumonia</i> LCP Protein Psr<sub>Sp</sub> Indicate the Importance of Dynamics in Four Long Loops for Ligand Specificity

The crystal structure of the extracellular region of the second pneumococcal LCP, a polyisoprenyl-teichoic acid-peptidoglycan teichoic acid transferase Psr<sub>Sp</sub>, was determined and refined to 2.15 Å resolution. Despite the low sequence homology with other LCP proteins, the Psr<...

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Main Authors: Tatyana Sandalova, Benedetta Maria Sala, Martin Moche, Hans-Gustaf Ljunggren, Evren Alici, Birgitta Henriques-Normark, Tatiana Agback, Dmitry Lesovoy, Peter Agback, Adnane Achour
Format: Article
Language:English
Published: MDPI AG 2024-12-01
Series:Crystals
Subjects:
<i>S. pneumoniae</i>
LCP
cell wall teichoic acid
capsular polysaccharide
crystal structure
NMR
Online Access:https://www.mdpi.com/2073-4352/14/12/1094
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Summary:The crystal structure of the extracellular region of the second pneumococcal LCP, a polyisoprenyl-teichoic acid-peptidoglycan teichoic acid transferase Psr<sub>Sp</sub>, was determined and refined to 2.15 Å resolution. Despite the low sequence homology with other LCP proteins, the Psr<sub>Sp</sub> maintains the fold of the LCP domain, and the positions of the residues suggested to participate in the transferase function are conserved. The tunnel found in the Psr<sub>Sp</sub> between the central β-sheet and three α-helices is wide enough to accommodate polyisoprenyl-teichoic acid. Comparison of the crystallographic temperature factors of LCP from distinct bacteria demonstrated that the four long loops located close to the teichoic acid and peptidoglycan binding sites have different relative mobilities. To compare the dynamics of the Psr<sub>Sp</sub> in crystalline state and in solution, NMR spectra were recorded, and 88% of the residues were assigned in the <sup>1</sup>H-<sup>15</sup>N TROSY HSQC spectra. Perfect accordance in the secondary structure of the crystal structure of Psr<sub>Sp</sub> with NMR data demonstrated correct assignment. Moreover, the relative mobility of the essential loops estimated from the crystallographic B-factor is in good agreement with order parameter S<sup>2</sup>, predicted from chemical shift. We hypothesize that the dynamics of these loops are important for the substrate promiscuity of LCP proteins.
ISSN:2073-4352

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