4tlw | pdb_00004tlw

CARDS TOXIN, FULL-LENGTH

spinqualitylabelsall models 4tlw, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tlw is a 1 chain structure with sequence from Mycoplasma pneumoniae M129. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARDS_MYCPN Acts as an ADP-ribosylating toxin, which may transfer the ADP-ribosyl group from NAD(+) to specific amino acids in target proteins. Elicits cytopathic effects in mammalian cells, such as disorganization and disruption of respiratory epithelial integrity in tracheal epithelium and vacuolization in the cytoplasm of CHO and HeLa cells. Publication Abstract from PubMed Mycoplasma pneumoniae (Mp) infections cause tracheobronchitis and "walking" pneumonia, and are linked to asthma and other reactive airway diseases. As part of the infectious process, the bacterium expresses a 591-aa virulence factor with both mono-ADP ribosyltransferase (mART) and vacuolating activities known as Community-Acquired Respiratory Distress Syndrome Toxin (CARDS TX). CARDS TX binds to human surfactant protein A and annexin A2 on airway epithelial cells and is internalized, leading to a range of pathogenetic events. Here we present the structure of CARDS TX, a triangular molecule in which N-terminal mART and C-terminal tandem beta-trefoil domains associate to form an overall architecture distinct from other well-recognized ADP-ribosylating bacterial toxins. We demonstrate that CARDS TX binds phosphatidylcholine and sphingomyelin specifically over other membrane lipids, and that cell surface binding and internalization activities are housed within the C-terminal beta-trefoil domain. The results enhance our understanding of Mp pathogenicity and suggest a novel avenue for the development of therapies to treat Mp-associated asthma and other acute and chronic airway diseases. Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae.,Becker A, Kannan TR, Taylor AB, Pakhomova ON, Zhang Y, Somarajan SR, Galaleldeen A, Holloway SP, Baseman JB, Hart PJ Proc Natl Acad Sci U S A. 2015 Apr 6. pii: 201420308. PMID:25848012 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA