2v9h
From Proteopedia
SOLUTION STRUCTURE OF AN ESCHERICHIA COLI YAET TANDEM POTRA DOMAIN
Overview
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.
About this Structure
2V9H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes., Knowles TJ, Jeeves M, Bobat S, Dancea F, McClelland D, Palmer T, Overduin M, Henderson IR, Mol Microbiol. 2008 Apr 21;. PMID:18430136 Page seeded by OCA on Wed May 7 08:44:03 2008
