Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE

CS Rule, M Patrick, JL Camberg, N Maricic… - …, 2016 - Wiley Online Library
The type II secretion system Eps in Vibrio cholerae promotes the extracellular transport of
cholera toxin and several hydrolytic enzymes and is a major virulence system in many Gram …

In vivo cross‐linking of EpsG to EpsL suggests a role for EpsL as an ATPase‐pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae

MD Gray, M Bagdasarian, WGJ Hol… - Molecular …, 2011 - Wiley Online Library
The type II secretion system is a multi‐protein complex that spans the cell envelope of Gram‐
negative bacteria and promotes the secretion of proteins, including several virulence factors …

Molecular Analysis of the Vibrio cholerae Type II Secretion ATPase EpsE

JL Camberg, M Sandkvist - Journal of bacteriology, 2005 - Am Soc Microbiol
The type II secretion system is a macromolecular assembly that facilitates the extracellular
translocation of folded proteins in gram-negative bacteria. EpsE, a member of this secretion …

Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity

M Patrick, KV Korotkov, WGJ Hol… - Journal of Biological …, 2011 - ASBMB
EpsE is an ATPase that powers transport of cholera toxin and hydrolytic enzymes through
the Type II secretion (T2S) apparatus in the Gram-negative bacterium, Vibrio cholerae. On …

Mapping Critical Interactive Sites within the Periplasmic Domain of the Vibrio cholerae Type II Secretion Protein EpsM

TL Johnson, ME Scott, M Sandkvist - Journal of bacteriology, 2007 - Am Soc Microbiol
The type II secretion (T2S) system is present in many gram-negative species, both
pathogenic and nonpathogenic, where it supports the delivery of a variety of toxins …

The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae

J Abendroth, P Murphy, M Sandkvist… - Journal of molecular …, 2005 - Elsevier
Gram-negative bacteria use type II secretion systems for the transport of virulence factors
and hydrolytic enzymes through the outer membrane. These sophisticated multi-protein …

Analysis of the Crystal Structure of the ExsC·ExsE Complex Reveals Distinctive Binding Interactions of the Pseudomonas aeruginosa Type III Secretion Chaperone …

NJ Vogelaar, X Jing, HH Robinson, FD Schubot - Biochemistry, 2010 - ACS Publications
Pseudomonas aeruginosa, like many Gram-negative bacterial pathogens, requires its type
III secretion system (T3SS) to facilitate acute infections. In P. aeruginosa, the expression of …

Identification of XcpZ Domains Required for Assembly of the Secreton of Pseudomonas aeruginosa

V Robert, F Hayes, A Lazdunski… - Journal of …, 2002 - Am Soc Microbiol
Most of the exoproteins secreted by Pseudomonas aeruginosa are transported via the type II
secretion system. This machinery, which is widely conserved in gram-negative bacteria …

Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae

ME Yanez, KV Korotkov, J Abendroth… - Journal of molecular …, 2008 - Elsevier
Many Gram-negative bacteria use the multi-protein type II secretion system (T2SS) to
selectively translocate virulence factors from the periplasmic space into the extracellular …

The 1.59 Å resolution structure of the minor pseudopilin EpsH of Vibrio cholerae reveals a long flexible loop

K Raghunathan, FS Vago, D Grindem, T Ball… - … et Biophysica Acta (BBA …, 2014 - Elsevier
The type II secretion complex exports folded proteins from the periplasm to the extracellular
milieu. It is used by the pathogenic bacterium Vibrio cholerae to export several proteins …