 |
PDBsum entry 4zv0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
4zv0
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
An interbacterial NAD(p)(+) glycohydrolase toxin requires elongation factor tu for delivery to target cells.
|
|
|
Authors
|
|
J.C.Whitney,
D.Quentin,
S.Sawai,
M.Leroux,
B.N.Harding,
H.E.Ledvina,
B.Q.Tran,
H.Robinson,
Y.A.Goo,
D.R.Goodlett,
S.Raunser,
J.D.Mougous.
|
|
|
Ref.
|
|
Cell, 2015,
163,
607-619.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Type VI secretion (T6S) influences the composition of microbial communities by
catalyzing the delivery of toxins between adjacent bacterial cells. Here, we
demonstrate that a T6S integral membrane toxin from Pseudomonas aeruginosa,
Tse6, acts on target cells by degrading the universally essential dinucleotides
NAD(+) and NADP(+). Structural analyses of Tse6 show that it resembles
mono-ADP-ribosyltransferase proteins, such as diphtheria toxin, with the
exception of a unique loop that both excludes proteinaceous ADP-ribose acceptors
and contributes to hydrolysis. We find that entry of Tse6 into target cells
requires its binding to an essential housekeeping protein, translation
elongation factor Tu (EF-Tu). These proteins participate in a larger assembly
that additionally directs toxin export and provides chaperone activity.
Visualization of this complex by electron microscopy defines the architecture of
a toxin-loaded T6S apparatus and provides mechanistic insight into intercellular
membrane protein delivery between bacteria.
|
|
|
|
|
|
|
