Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans

Autor: Patrick Weber, Mireille Nowakowski, Isabelle Miras, Mathieu Picardeau, William Shepard, Frederick Saul, Ahmed Haouz
Přispěvatelé: Cristallographie (Plateforme) - Crystallography (Platform), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Production de Protéines Recombinantes (Plate-Forme) (PRPF), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Biologie des Spirochètes / Biology of Spirochetes, Institut Pasteur [Paris], This work was supported by the Institut Pasteur and the French Ministry of Research (ANR-08-MIE-018)., We acknowledge access to the PROXIMA1 beamline at SOLEIL and the support from its staff. We thank Jacques Bellalou for assistance in protein-production optimization and Vincent Bondet for protein purification at an early stage of the work (PFPR, Institut Pasteur), ANR-08-MIEN-0018,LEPTOVIR,Les leptospires : de la génétique à la pathogénèse(2008), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)
Jazyk: angličtina
Rok vydání: 2015
Předmět:
LRR motif
crystal structure
MESH: Leptospira interrogans/chemistry
Subfamily
Protein Conformation
[SDV]Life Sciences [q-bio]
Molecular Sequence Data
Human pathogen
chemical and pharmacologic phenomena
spirochaetes
MESH: Amino Acid Sequence
medicine.disease_cause
Crystallography
X-Ray
Leucine-Rich Repeat Proteins
Genome
Microbiology
03 medical and health sciences
MESH: Protein Conformation
Bacterial Proteins
Structural Biology
Leptospira
medicine
MESH: Proteins/genetics
MESH: Cloning
Molecular
Amino Acid Sequence
Cloning
Molecular
Structural motif
Gene
MESH: Bacterial Proteins
030304 developmental biology
Genetics
0303 health sciences
MESH: Molecular Sequence Data
biology
030306 microbiology
fungi
Proteins
Pathogenic bacteria
General Medicine
biology.organism_classification
MESH: Crystallography
X-Ray
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
Leptospira interrogans
Zdroj: Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2015, 71 (6), pp.1351-1359. ⟨10.1107/S139900471500704X⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (6), pp.1351-1359. ⟨10.1107/S139900471500704X⟩
ISSN: 0907-4449
2059-7983
DOI: 10.1107/S139900471500704X⟩
Popis: Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic α/β-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria.
Databáze: OpenAIRE
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