4OOJ

Crystal structure of the N-terminal domain of the Legionella pneumophila protein SidC at 2.4A resolution

Summary for 4OOJ

• Entry DOI: 10.2210/pdb4ooj/pdb
• Descriptor: SidC, interaptin, MAGNESIUM ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: novel fold, legionella effector, legionella containing vacuole, host-pathogen interaction, unknown function
• Biological source: Legionella pneumophila
• Total number of polymer chains: 4
• Total formula weight: 282411.92

Authors

Gazdag, E.M.,Shoebel, S.,Shkumatov, A.V.,Goody, R.S.,Itzen, A. (deposition date: 2014-02-03, release date: 2014-02-26, Last modification date: 2024-04-03)

Primary citation

Gazdag, E.M.,Schobel, S.,Shkumatov, A.V.,Goody, R.S.,Itzen, A.
The structure of the N-terminal domain of the Legionella protein SidC
J.Struct.Biol., 186:188-194, 2014

PubMed Abstract: The Gram-negative bacterium Legionella pneumophila is the causative agent of Legionnaires' disease. During infection of eukaryotic cells, the bacterium releases about 300 different bacterial effector molecules that aid in the establishment of the Legionella-containing vacuole (LCV) among which SidC is one of these secreted proteins. However, apart from membrane lipid binding the function of SidC remains elusive. In order to characterize SidC further, we have determined the crystal structure of the N-terminal domain of SidC (amino acids 1-609, referred to as SidC-N) at 2.4Å resolution. SidC-N reveals a novel fold in which 4 potential subdomains (A-D) are arranged in a crescent-like structure. None of these subdomains currently has any known structural homologues, raising the question of how this fold has evolved. These domains are highly interconnected, with a low degree of flexibility towards each other. Due to the extended arrangement of the subdomains, SidC-N may contain multiple binding sites for potential interaction partners.

PubMed: 24556577
DOI: 10.1016/j.jsb.2014.02.003

Experimental method

X-RAY DIFFRACTION (2.4 Å)