2yny

Salmonella enterica SadA 255-302 fused to GCN4 adaptors (SadAK1)

spinqualitylabelsall models 2yny, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yny is a 3 chain structure with sequence from Saccharomyces cerevisiae and Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SADA_SALTY Involved in cell aggregation, biofilm formation, and adhesion to human intestinal epithelial cells. GCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. Publication Abstract from PubMed Trimeric autotransporter adhesins (TAAs) are modular, highly repetitive surface proteins that mediate adhesion to host cells in a broad range of Gram-negative pathogens. Although their sizes may differ by more than one order of magnitude, they all follow the same basic head-stalk-anchor architecture, where the head mediates adhesion and autoagglutination, the stalk projects the head from the bacterial surface, and the anchor provides the export function and attaches the adhesin to the bacterial outer membrane after export is complete. In complex adhesins, head and stalk domains may alternate several times before the anchor is reached. Despite extensive sequence divergence, the structures of TAA domains are highly constrained, due to the tight interleaving of their constituent polypeptide chains. We have therefore taken a "domain dictionary" approach to characterize representatives for each domain type by X-ray crystallography and use these structures to reconstruct complete TAA fibers. With SadA from Salmonella enterica, EhaG from enteropathogenic Escherichia coli (EHEC), and UpaG from uropathogenic E. coli (UPEC), we present three representative structures of a complex adhesin that occur in a conserved genomic context in Enterobacteria and is essential in the infection process of uropathogenic E. coli. Our work proves the applicability of the dictionary approach to understanding the structure of a class of proteins that are otherwise poorly tractable by high-resolution methods and provides a basis for the rapid and detailed annotation of newly identified TAAs. Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria.,Hartmann MD, Grin I, Dunin-Horkawicz S, Deiss S, Linke D, Lupas AN, Hernandez Alvarez B Proc Natl Acad Sci U S A. 2012 Dec 18;109(51):20907-12. doi:, 10.1073/pnas.1211872110. Epub 2012 Dec 3. PMID:23213248 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gcn4 3D Structures Gnc4 3D Structures

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