4AUR

LeoA bacterial dynamin GTPase from ETEC

Summary for 4AUR

• Entry DOI: 10.2210/pdb4aur/pdb
• Descriptor: LEOA, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase, lt toxin
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 65913.23

Authors

Michie, K.A.,Low, H.H.,Lowe, J. (deposition date: 2012-05-21, release date: 2013-08-28, Last modification date: 2014-10-22)

Primary citation

Michie, K.A.,Boysen, A.,Low, H.H.,Moller-Jensen, J.,Lowe, J.
Leoa, B and C from Enterotoxigenic Escherichia Coli (Etec) are Bacterial Dynamins.
Plos One, 9:07211-, 2014

PubMed Abstract: Escherichia coli (ETEC) strain H10407 contains a GTPase virulence factor, LeoA, which is encoded on a pathogenicity island and has been shown to enhance toxin release, potentially through vesicle secretion. By sequence comparisons and X-ray structure determination we now identify LeoA as a bacterial dynamin-like protein (DLP). Proteins of the dynamin family remodel membranes and were once thought to be restricted to eukaryotes. In ETEC H10407 LeoA localises to the periplasm where it forms a punctate localisation pattern. Bioinformatic analyses of leoA and the two upstream genes leoB and leoC suggest that LeoA works in concert with a second dynamin-like protein, made up of LeoB and LeoC. Disruption of the leoAB genes leads to a reduction in secretion of periplasmic Tat-GFP and outer membrane OmpA. Our data suggest a role for LeoABC dynamin-like proteins in potentiating virulence through membrane vesicle associated toxin secretion.

PubMed: 25203511
DOI: 10.1371/JOURNAL.PONE.0107211

Experimental method

X-RAY DIFFRACTION (2.7 Å)