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5BQ9

Crystal structure of uncharacterized protein lpg1496 Legionella pneumophila subsp. pneumophila

Summary for 5BQ9
Entry DOI10.2210/pdb5bq9/pdb
DescriptorUncharacterized protein (2 entities in total)
Functional Keywordsstructural genomics, psi-biology, midwest center for structural genomics, mcsg, unknown function
Biological sourceLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Total number of polymer chains2
Total formula weight136014.81
Authors
Chang, C.,Morar, M.,Evdokimova, E.,Savchenko, A.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2015-05-28, release date: 2015-06-10, Last modification date: 2024-11-20)
Primary citationMorar, M.,Evdokimova, E.,Chang, C.,Ensminger, A.W.,Savchenko, A.
Crystal structure of the Legionella pneumophila lem10 effector reveals a new member of the HD protein superfamily.
Proteins, 83:2319-2325, 2015
Cited by
PubMed 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.
PubMed: 26426142
DOI: 10.1002/prot.24933
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2785 Å)
Structure validation

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