title: The structure of the N-terminal domain of the Legionella protein SidC.
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.
authors.affiliation: Max Planck Institute of Molecular Physiology, Department of Physical Biochemistry, Dortmund 44227, Germany.
authors.forename: Emerich Mihai
authors.initials: EM
authors.lastname: Gazdag
authors.affiliation: Max Planck Institute of Molecular Physiology, Department of Physical Biochemistry, Dortmund 44227, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Schöbel
authors.affiliation: Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, Herestraat 49, 3000 Leuven, Belgium.
authors.forename: Alexander V
authors.initials: AV
authors.lastname: Shkumatov
authors.affiliation: Max Planck Institute of Molecular Physiology, Department of Physical Biochemistry, Dortmund 44227, Germany. Electronic address: roger.goody@mpi-dortmund.mpg.de.
authors.forename: Roger S
authors.initials: RS
authors.lastname: Goody
authors.affiliation: Center for Integrated Protein Science Munich, Chemistry Department, Technische Universität München, Lichtenbergstr. 4, 85748 Garching, Germany. Electronic address: aymelt.itzen@tum.de.
authors.forename: Aymelt
authors.initials: A
authors.lastname: Itzen
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D016952:Legionella pneumophila; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D053838:Scattering, Small Angle
chemical_list: D001426:Bacterial Proteins; C534216:SidC protein, Legionella pneumophila
keywords: Effector; Legionella; Legionella containing vacuole; SidC