Crystal structure of the N‐terminal domain of the fibronectin‐binding protein PavA from Streptococcus pneumoniae. Issue 10 (4th October 2019)

• Record Type: Journal Article
• Authors: Manne, Kartik; Narayana, Sthanam V. L.; Chattopadhyay, Debasish
• Is Part Of: Acta crystallographica. Volume 75:Issue 10(2019:Oct.)
• Page Start: 657
• Page End: 662
• Publication Date: 2019-10-04
• Subjects: fibronectin‐binding protein -- Streptococcus pneumoniae -- X‐ray crystallography -- pneumococcal adherence and virulence factor A -- PavA -- crystal structure; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X19012160
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : Pneumococcal adherence and virulence factor A (PavA) plays a key role in the adhesion of Streptococcus pneumoniae to host tissues. Here, the crystal structure of the N‐terminal domain of PavA is presented, which reveals structural differences from its homologs. 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.