4R0G

Crystal structure of Lpg0393 from Legionella pneumophila

Summary for 4R0G

• Entry DOI: 10.2210/pdb4r0g/pdb
• Descriptor: Uncharacterized protein (1 entity in total)
• Functional Keywords: vps9, gef, unknown function
• Biological source: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
• Total number of polymer chains: 4
• Total formula weight: 133829.48

Authors

Sohn, Y.S.,Shin, H.C.,Oh, B.H. (deposition date: 2014-07-31, release date: 2015-04-15, Last modification date: 2024-03-20)

Primary citation

Sohn, Y.S.,Shin, H.C.,Park, W.S.,Ge, J.,Kim, C.H.,Lee, B.L.,Heo, W.D.,Jung, J.U.,Rigden, D.J.,Oh, B.H.
Lpg0393 of Legionella pneumophila Is a Guanine-Nucleotide Exchange Factor for Rab5, Rab21 and Rab22
Plos One, 10:e0118683-e0118683, 2015

PubMed Abstract: Legionella pneumophila, a human intracellular pathogen, encodes about 290 effector proteins that are translocated into host cells through a secretion machinery. Some of these proteins have been shown to manipulate or subvert cellular processes during infection, but functional roles of a majority of them remain unknown. Lpg0393 is a newly identified Legionella effector classified as a hypothetical protein. Through X-ray crystallographic analysis, we show that Lpg0393 contains a Vps9-like domain, which is structurally most similar to the catalytic core of human Rabex-5 that activates the endosomal Rab proteins Rab5, Rab21 and Rab22. Consistently, Lpg0393 exhibited a guanine-nucleotide exchange factor activity toward the endosomal Rabs. This work identifies the first example of a bacterial guanine-nucleotide exchange factor that is active towards the Rab5 sub-cluster members, implying that the activation of these Rab proteins might be advantageous for the intracellular survival of Legionella.

PubMed: 25821953
DOI: 10.1371/journal.pone.0118683

Experimental method

X-RAY DIFFRACTION (2.7 Å)