5h3x

The structure of the N-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)

spinqualitylabelsall models 5h3x, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h3x is a 1 chain structure with sequence from Streptococcus suis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RQCH_STRSY Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844] Publication Abstract from PubMed The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 A, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via beta1 integrin receptors to induce chemokine production. Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.,Musyoki AM, Shi Z, Xuan C, Lu G, Qi J, Gao F, Zheng B, Zhang Q, Li Y, Haywood J, Liu C, Yan J, Shi Y, Gao GF Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13869-13874. Epub 2016 Nov 10. PMID:27834729 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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