Structural highlights
Publication Abstract from PubMed
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 A is reported. Each monomer of the dimeric protein consists of two domains (domains I and II) and a short alpha-helix (alpha6) 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 alpha5, alpha6 and the domain II/alpha6 inter-loop region within domain II. The alpha5 helix of FBPS-N folds back toward domain I, whereas in SpPavA-N it adopts an elongated rod shape.
Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae.,Manne K, Narayana SVL, Chattopadhyay D Acta Crystallogr F Struct Biol Commun. 2019 Oct 1;75(Pt 10):657-662. doi:, 10.1107/S2053230X19012160. Epub 2019 Sep 24. PMID:31584015[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Manne K, Narayana SVL, Chattopadhyay D. Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae. Acta Crystallogr F Struct Biol Commun. 2019 Oct 1;75(Pt 10):657-662. doi:, 10.1107/S2053230X19012160. Epub 2019 Sep 24. PMID:31584015 doi:http://dx.doi.org/10.1107/S2053230X19012160
