The structure of the N-terminal domain of the Legionella protein SidC

Emerich Mihai Gazdag; Stefan Schöbel; Alexander V Shkumatov; Roger S Goody; Aymelt Itzen

doi:10.1016/j.jsb.2014.02.003

The structure of the N-terminal domain of the Legionella protein SidC

Standard

The structure of the N-terminal domain of the Legionella protein SidC. / Gazdag, Emerich Mihai; Schöbel, Stefan; Shkumatov, Alexander V; Goody, Roger S; Itzen, Aymelt.

in: J STRUCT BIOL, Jahrgang 186, Nr. 1, 04.2014, S. 188-94.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Gazdag, EM, Schöbel, S, Shkumatov, AV, Goody, RS & Itzen, A 2014, 'The structure of the N-terminal domain of the Legionella protein SidC', J STRUCT BIOL, Jg. 186, Nr. 1, S. 188-94. https://doi.org/10.1016/j.jsb.2014.02.003

APA

Gazdag, E. M., Schöbel, S., Shkumatov, A. V., Goody, R. S., & Itzen, A. (2014). The structure of the N-terminal domain of the Legionella protein SidC. J STRUCT BIOL, 186(1), 188-94. https://doi.org/10.1016/j.jsb.2014.02.003

Vancouver

Gazdag EM, Schöbel S, Shkumatov AV, Goody RS, Itzen A. The structure of the N-terminal domain of the Legionella protein SidC. J STRUCT BIOL. 2014 Apr;186(1):188-94. https://doi.org/10.1016/j.jsb.2014.02.003

Bibtex

@article{59cb9d3abab743e28561851c65fc8b12,

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 2.4{\AA} 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. ",

keywords = "Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Legionella pneumophila, Models, Molecular, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Scattering, Small Angle, Journal Article",

author = "Gazdag, {Emerich Mihai} and Stefan Sch{\"o}bel and Shkumatov, {Alexander V} and Goody, {Roger S} and Aymelt Itzen",

year = "2014",

month = apr,

doi = "10.1016/j.jsb.2014.02.003",

language = "English",

volume = "186",

pages = "188--94",

journal = "J STRUCT BIOL",

issn = "1047-8477",

publisher = "Academic Press Inc.",

number = "1",

}

RIS

TY - JOUR

T1 - The structure of the N-terminal domain of the Legionella protein SidC

AU - Gazdag, Emerich Mihai

AU - Schöbel, Stefan

AU - Shkumatov, Alexander V

AU - Goody, Roger S

AU - Itzen, Aymelt

PY - 2014/4

Y1 - 2014/4

N2 - 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.

AB - 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.

KW - Bacterial Proteins

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Legionella pneumophila

KW - Models, Molecular

KW - Protein Interaction Domains and Motifs

KW - Protein Structure, Secondary

KW - Scattering, Small Angle

KW - Journal Article

U2 - 10.1016/j.jsb.2014.02.003

DO - 10.1016/j.jsb.2014.02.003

M3 - SCORING: Journal article

C2 - 24556577

VL - 186

SP - 188

EP - 194

JO - J STRUCT BIOL

JF - J STRUCT BIOL

SN - 1047-8477

IS - 1

ER -