4L6T

GM1 bound form of the ECX AB5 holotoxin

Summary for 4L6T

• Entry DOI: 10.2210/pdb4l6t/pdb
• Related: 2wv6 4L63
• Descriptor: ECXA, ECXB, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: cholera-like toxin, matrix metalloproteinase, bacterial mmp, metzincin, ab5, ob fold, transferase, toxin, protease, pentasacharide, gm1, ganglioside, oligosaccharide complex, toxilysin, hydrolase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 6
• Total formula weight: 98430.05

Authors

Littler, D.R.,Ng, N.M.,Rossjohn, J.,Beddoe, T. (deposition date: 2013-06-12, release date: 2013-11-06, Last modification date: 2024-10-30)

Primary citation

Ng, N.M.,Littler, D.R.,Paton, A.W.,Le Nours, J.,Rossjohn, J.,Paton, J.C.,Beddoe, T.
EcxAB Is a Founding Member of a New Family of Metalloprotease AB5 Toxins with a Hybrid Cholera-like B Subunit.
Structure, 21:2003-2013, 2013

PubMed Abstract: AB5 toxins are composed of an enzymatic A subunit that disrupts cellular function associated with a pentameric B subunit required for host cell invasion. EcxAB is an AB5 toxin isolated from clinical strains of Escherichia coli classified as part of the cholera family due to B subunit homology. Cholera-group toxins have catalytic ADP-ribosyltransferases as their A subunits, so it was surprising that EcxA did not. We confirmed that EcxAB self-associates as a functional toxin and obtained its structure. EcxAB is a prototypical member of a hybrid AB5 toxin family containing metzincin-type metalloproteases as their active A subunit paired to a cholera-like B subunit. Furthermore, EcxA is distinct from previously characterized proteases and thus founds an AB5-associated metzincin family that we term the toxilysins. EcxAB provides the first observation of conserved B subunit usage across different AB5 toxin families and provides evidence that the intersubunit interface of these toxins is far more permissive than previously supposed.

PubMed: 24095060
DOI: 10.1016/j.str.2013.08.024

Experimental method

X-RAY DIFFRACTION (1.859 Å)