Structure-function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G-proteins
Dene R Littler, Sheng Y Ang, Danilo G Moriel, Martina Kocan, Oded Kleifeld, Matthew D Johnson, Mai T Tran, Adrienne W Paton, James C Paton, Roger J Summers, Mark A Schembri, Jamie Rossjohn, Travis Beddoe
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2017
Awarded by National Institutes of Health
We thank the staff of beamline MX2 at the Australian Synchrotron for assistance with X-ray data collection. We acknowledge the Consortium for Functional Glycomics funded by National Institutes of Health Grants GM62116 and GM98791 NIGMS for services provided by the Glycan Array Synthesis Core (The Scripps Research Institute, La Jolla, CA) that produced the mammalian glycan microarray and the Protein-Glycan Interaction Core (Emory University School of Medicine, Atlanta, GA) that assisted with analysis of samples on the array. We thank Natasha Ng for initially cloning EcPltAB.