Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae
| Autor: | Sthanam V.L. Narayana, Kartik Manne, Debasish Chattopadhyay |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Streptococcus suis Biophysics medicine.disease_cause Crystallography X-Ray Biochemistry Virulence factor Microbiology Research Communications 03 medical and health sciences Bacterial Proteins Protein Domains Structural Biology Streptococcus pneumoniae Genetics medicine Cell adhesion Adhesins Bacterial 030304 developmental biology 0303 health sciences biology Chemistry 04 agricultural and veterinary sciences Condensed Matter Physics biology.organism_classification Recombinant Proteins Fibronectin binding Structural Homology Protein Helix Domain (ring theory) 040102 fisheries 0401 agriculture forestry and fisheries Bacteria |
| Zdroj: | Acta Crystallogr F Struct Biol Commun |
| Popis: | The Gram-positive bacteriumStreptococcus pneumoniae, a major human pathogen, is a regular colonizer of the upper and lower respiratory tracts. Pneumococcal adherence and virulence factor A (PavA), a fibronectin-binding bacterial protein, fromS. pneumoniaeis an important facilitator of its colonization of host cells. In this study, the crystal structure of the N-terminal domain of PavA (SpPavA-N) determined at a resolution of 2.39 Å is reported. Each monomer of the dimeric protein consists of two domains (domains I and II) and a short α-helix (α6) at the C-terminus that are connected by elongated loops. Comparison of the SpPavA-N structure with that of its homolog fromStreptococcus suis(FBPS-N) revealed differences in α5, α6 and the domain II/α6 inter-loop region within domain II. The α5 helix of FBPS-N folds back toward domain I, whereas in SpPavA-N it adopts an elongated rod shape. |
| Databáze: | OpenAIRE |
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