2YO0

Salmonella enterica SadA 1049-1304 fused to GCN4 adaptors (SadAK9-cfI)

Summary for 2YO0

• Entry DOI: 10.2210/pdb2yo0/pdb
• Related: 1CE9 1DGC 1FAV 1FMH 1GCL 1GCM 1GK6 1GZL 1IHQ 1IJ0 1IJ1 1IJ2 1IJ3 1KQL 1LD4 1LLM 1NKN 1PIQ 1RB1 1RB4 1RB5 1RB6 1SWI 1TMZ 1UNT 1UNU 1UNV 1UNW 1UNX 1UNY 1UNZ 1UO0 1UO1 1UO2 1UO3 1UO4 1UO5 1W5G 1W5H 1W5I 1W5J 1W5K 1W5L 1YSA 1ZII 1ZIJ 1ZIK 1ZIL 1ZIM 1ZTA 2B1F 2B22 2BNI 2CCE 2CCF 2CCN 2D3E 2DGC 2WG5 2WG6 2WPQ 2WPR 2WPS 2WPY 2WPZ 2WQ0 2WQ1 2WQ2 2WQ3 2YNZ 2YO1 2YO2 2YO3 2ZTA
• Descriptor: GENERAL CONTROL PROTEIN GCN4, PUTATIVE INNER MEMBRANE PROTEIN, CHLORIDE ION (3 entities in total)
• Functional Keywords: hans motif, yada-like head, ylhead, head insert motif, him, trimeric autotransporter adhesin, taa, membrane protein, chimera
• Biological source: SACCHAROMYCES CEREVISIAE; More
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 1
• Total formula weight: 34040.85

Authors

Hartmann, M.D.,Hernandez Alvarez, B.,Lupas, A.N. (deposition date: 2012-10-20, release date: 2012-12-12, Last modification date: 2023-12-20)

Primary citation

Hartmann, M.D.,Grin, I.,Dunin-Horkawicz, S.,Deiss, S.,Linke, D.,Lupas, A.N.,Hernandez Alvarez, B.
Complete Fiber Structures of Complex Trimeric Autotransporter Adhesins Conserved in Enterobacteria.
Proc.Natl.Acad.Sci.USA, 109:20907-, 2012

PubMed Abstract: 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.

PubMed: 23213248
DOI: 10.1073/PNAS.1211872110

Experimental method

X-RAY DIFFRACTION (2.8 Å)