 |
PDBsum entry 2v9h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
2v9h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Fold and function of polypeptide transport-Associated domains responsible for delivering unfolded proteins to membranes.
|
|
|
Authors
|
|
T.J.Knowles,
M.Jeeves,
S.Bobat,
F.Dancea,
D.Mcclelland,
T.Palmer,
M.Overduin,
I.R.Henderson.
|
|
|
Ref.
|
|
Mol Microbiol, 2008,
68,
1216-1227.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
Membranes of Gram-negative bacteria, mitochondria and chloroplasts receive and
fold beta-barrel transmembrane proteins through the action of polypeptide
transport-associated (POTRA) domains. In Escherichia coli, folding substrates
are inserted into the outer membrane by the essential protein YaeT, a prototypic
Omp85 protein. Here, the articulation between tandem POTRA domains in solution
is defined by nuclear magnetic resonance (NMR) spectroscopy, indicating an
unprecedented juxtaposition. The novel solution orientations of all five POTRA
domains are revealed by small-angle X-ray scattering of the entire 46 kDa
periplasmic region. NMR titration studies show that strands from YaeT's
canonical folding substrate, PhoE, bind non-specifically along alternating sides
of its mixed beta sheets, thus providing an ideal platform for helping to fold
nascent outer-membrane proteins. Together, this provides the first structural
model of how multiple POTRA domains recruit substrates from the periplasmic
solution into the outer membrane.
|
|
|
|
|
|
|
