Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae

Academic Article

Abstract

  • © 2019 International Union of Crystallography. 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.
  • Digital Object Identifier (doi)

    Author List

  • Manne K; Narayana SVL; Chattopadhyay D
  • Start Page

  • 657
  • End Page

  • 662
  • Volume

  • 75