Unknown

Dataset Information

0

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

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 ?-helix (?6) 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 ?5, ?6 and the domain II/?6 inter-loop region within domain II. The ?5 helix of FBPS-N folds back toward domain I, whereas in SpPavA-N it adopts an elongated rod shape.

SUBMITTER: Manne K 

PROVIDER: S-EPMC6777132 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Manne Kartik K   Narayana Sthanam V L SVL   Chattopadhyay Debasish D  

Acta crystallographica. Section F, Structural biology communications 20190924 Pt 10

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  ...[more]

Similar Datasets

Unknown The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin.
| S-EPMC3668722 | biostudies-literature
Unknown Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae.
| S-EPMC2658566 | biostudies-literature
Unknown Structure of the choline-binding domain of Spr1274 in Streptococcus pneumoniae.
| S-EPMC2720326 | biostudies-literature
Unknown Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity.
| S-EPMC2151468 | biostudies-literature
Unknown Crystal structure of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae reveals the binding mode of an inhibitor.
| S-EPMC2271168 | biostudies-literature
Unknown Breakage-reunion domain of Streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone target.
| S-EPMC1810434 | biostudies-literature
Unknown Glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae is membrane associated.
| S-EPMC93718 | biostudies-literature
Unknown Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca2+-binding module.
| S-EPMC3546320 | biostudies-literature
Unknown Extended binding site on fibronectin for the functional upstream domain of protein F1 of Streptococcus pyogenes.
| S-EPMC3003407 | biostudies-literature
Unknown SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen.
| S-EPMC115982 | biostudies-literature