Crystallization of FcpA from Leptospira, a novel flagellar protein that is essential for pathogenesis
Autor: | Alejandro Buschiazzo, Ariel E. Mechaly, Nicole Larrieux, Albert I. Ko, Fabiana San Martin, Elsio A. Wunder, Mathieu Picardeau, Felipe Trajtenberg |
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Přispěvatelé: | Molecular and structural microbiology / Microbiología Molecular y Estructural [Montevideo], Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Yale School of Public Health (YSPH), Fundação Oswaldo Cruz (FIOCRUZ), Réseau International des Instituts Pasteur (RIIP), Biologie des Spirochètes / Biology of Spirochetes, Institut Pasteur [Paris], Integrative Microbiology of Zoonotic Agents [Paris and Montevideo] (IMiZA), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur [Paris], Fundação Oswaldo Cruz / Oswaldo Cruz Foundation (FIOCRUZ), Institut Pasteur [Paris] (IP), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur [Paris] (IP) |
Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
MESH: Leptospira interrogans MESH: Sequence Homology Amino Acid Protein Data Bank (RCSB PDB) Gene Expression MESH: Amino Acid Sequence Crystallography X-Ray medicine.disease_cause Biochemistry MESH: Leptospira MESH: Recombinant Proteins Plasmid Structural Biology leptospirosis spirochetes Cloning Molecular Peptide sequence MESH: Bacterial Proteins Leptospira biology Chemistry MESH: Escherichia coli Condensed Matter Physics Recombinant Proteins motility SAD phasing flagella Leptospira interrogans Plasmids MESH: Gene Expression FcpA Biophysics MESH: Sequence Alignment Sequence alignment Flagellum Leptospira biflexa MESH: Flagella Article 03 medical and health sciences Bacterial Proteins MESH: Plasmids Escherichia coli Genetics medicine [CHIM.CRIS]Chemical Sciences/Cristallography MESH: Cloning Molecular Amino Acid Sequence [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Sequence Homology Amino Acid biology.organism_classification MESH: Crystallography X-Ray [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology 030104 developmental biology Sequence Alignment |
Zdroj: | Acta crystallographica. Section F, Structural biology communications Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd, 2017, 73 (3), pp.123-129. ⟨10.1107/S2053230X17002096⟩ Acta crystallographica Section F : Structural biology communications [2014-...] Acta crystallographica Section F : Structural biology communications [2014-..], 2017, 73 (3), pp.123-129. ⟨10.1107/S2053230X17002096⟩ |
ISSN: | 2053-230X |
Popis: | The protein FcpA is a unique component of the flagellar filament of spirochete bacteria belonging to the genusLeptospira. Although it plays an essential role in translational motility and pathogenicity, no structures of FcpA homologues are currently available in the PDB. Its three-dimensional structure will unveil the novel motility mechanisms that render pathogenicLeptospiraparticularly efficient at invading and disseminating within their hosts, causing leptospirosis in humans and animals. FcpA fromL. interroganswas purified and crystallized, but despite laborious attempts no useful X ray diffraction data could be obtained. This challenge was solved by expressing a close orthologue from the related saprophytic speciesL. biflexa. Three different crystal forms were obtained: a primitive and a centred monoclinic form, as well as a hexagonal variant. All forms diffracted X-rays to suitable resolutions for crystallographic analyses, with the hexagonal type typically reaching the highest limits of 2.0 Å and better. A variation of the quick-soaking procedure resulted in an iodide derivative that was instrumental for single-wavelength anomalous diffraction methods. |
Databáze: | OpenAIRE |
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