6PON

CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF FIBRONECTIN- BINDING PROTEIN PAVA FROM STREPTOCOCCUS PNEUMONIAE

Summary for 6PON

• Entry DOI: 10.2210/pdb6pon/pdb
• Descriptor: Adherence and virulence protein A (2 entities in total)
• Functional Keywords: fibronectin-binding protein, pneumococcal adherence and virulence factor a, pava, cell adhesion
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 62897.29

Authors

Manne, K.,Narayana, S.V.L. (deposition date: 2019-07-04, release date: 2019-07-31, Last modification date: 2023-10-11)

Primary citation

Manne, K.,Narayana, S.V.L.,Chattopadhyay, D.
Crystal structure of the N-terminal domain of the fibronectin-binding protein PavA from Streptococcus pneumoniae.
Acta Crystallogr.,Sect.F, 75:657-662, 2019

PubMed 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.

PubMed: 31584015
DOI: 10.1107/S2053230X19012160

Experimental method

X-RAY DIFFRACTION (2.395 Å)