5BQ9: Crystal Structure Of Uncharacterized Protein Lpg1496 Legionella Pneumophila Subsp. Pneumophila

Citation:
Abstract
Legionella pneumophila, the intracellular pathogen that can cause severe pneumonia known as Legionnaire's disease, translocates close to 300 effectors inside the host cell using Dot/Icm type IVB secretion system. The structure and function for the majority of these effector proteins remains unknown. Here, we present the crystal structure of the L. pneumophila effector Lem10. The structure reveals a multidomain organization with the largest C-terminal domain showing strong structural similarity to the HD protein superfamily representatives. However, Lem10 lacks the catalytic His-Asp residue pair and does not show any in vitro phosphohydrolase enzymatic activity, typical for HD proteins. While the biological function of Lem10 remains elusive, our analysis shows that similar distinct features are shared by a significant number of HD domains found in Legionella proteins, including the SidE family of effectors known to play an important role during infection. Taken together our data point to the presence of a specific group of non-catalytic Legionella HD domains, dubbed LHDs, which are involved in pathogenesis. Proteins 2015; 83:2319-2325. (c) 2015 Wiley Periodicals, Inc.
PDB ID: 5BQ9Download
MMDB ID: 130019
PDB Deposition Date: 2015/5/28
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 2.28  Å
Source Organism:
Similar Structures:
Biological Unit for 5BQ9: monomeric; determined by software (PISA)
Molecular Components in 5BQ9
Label Count Molecule
Protein (1 molecule)
1
Uncharacterized Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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