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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Bibliographic Details
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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https://www.mdpi.com/2073-4352/14/12/1094

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