Sticky socks: Helicobacter pylori VacA takes shape.
Several receptors have been described for the Helicobacter pylori vacuolating toxin VacA, which exerts different effects on epithelial cells and on immune cells. The crystal structure of the putative receptor-binding domain of VacA (p55) has now been solved. It consists of a parallel beta-helix with a C-terminal globular domain. A comparison between allelic variants of p55 and docking of the p55 domain into the quaternary structure, as shown by electron microscopy, revealed structural features that might be important for elucidating the molecular details of receptor interaction and channel formation.
Sewald
Xaver
X
Max von Pettenkofer-Institute for Hygiene and Medical Microbiology, Ludwig-Maximilians-University, Pettenkoferstrasse 9a, D-80336 Munich, Germany.
Fischer
Wolfgang
W
Haas
Rainer
R
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; C074689:VacA protein, Helicobacter pylori