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- Title
Crystal structure of the N‐terminal domain of the fibronectin‐binding protein PavA from Streptococcus pneumoniae.
- Authors
Manne, Kartik; Narayana, Sthanam V. L.; Chattopadhyay, Debasish
- Abstract
The Gram‐positive bacterium Streptococcus 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, from S. pneumoniae is 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 from Streptococcus 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.
- Subjects
STREPTOCOCCUS pneumoniae; CRYSTAL structure; PROTEIN domains; STREPTOCOCCUS suis; BACTERIAL proteins; FIBRONECTINS
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2019, Vol 75, Issue 10, p657
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X19012160