title: Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae.
abstract: The metalloprotease PrtV from Vibrio cholerae serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre-pro-protein that undergoes several N- and C-terminal modifications to form a catalytically active protease. We report here the NMR structure of the PrtV N-terminal domain (residues 23-103) that contains two short α-helices in a coiled coil motif. The helices are held together by a cluster of hydrophobic residues. Approximately 30 residues at the C-terminal end, which were predicted to form a third helical structure, are disordered. These residues are highly conserved within the genus Vibrio, which suggests that they might be functionally important.
authors.affiliation: Department of Chemistry, Umeå University, Umeå, SE-901 87, Sweden.|Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå, SE-901 87, Sweden.
authors.forename: Aaron
authors.initials: A
authors.lastname: Edwin
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, Gothenburg, SE-40530, Sweden.
authors.forename: Cecilia
authors.initials: C
authors.lastname: Persson
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, Gothenburg, SE-40530, Sweden.
authors.forename: Maxim
authors.initials: M
authors.lastname: Mayzel
authors.affiliation: Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå, SE-901 87, Sweden.|Department of Molecular Biology, Umeå University, Umeå, SE-901 87, Sweden.|The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå, SE-901 87, Sweden.
authors.forename: Sun Nyunt
authors.initials: SN
authors.lastname: Wai
authors.affiliation: Department of Pharmacology and Clinical Neuroscience, Umeå University, Umeå, SE-901 85, Sweden.
authors.forename: Anders
authors.initials: A
authors.lastname: Öhman
authors.affiliation: Swedish NMR Centre at the University of Gothenburg, Gothenburg, SE-40530, Sweden.
authors.forename: B Göran
authors.initials: BG
authors.lastname: Karlsson
authors.affiliation: Department of Chemistry, Umeå University, Umeå, SE-901 87, Sweden.|Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå, SE-901 87, Sweden.
authors.forename: A Elisabeth
authors.initials: AE
authors.lastname: Sauer-Eriksson
mesh_terms: D020134:Catalytic Domain; D017124:Conserved Sequence; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010447:Peptide Hydrolases / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014734:Vibrio cholerae / Q000737:chemistry / Q000201:enzymology*
chemical_list: D010447:Peptide Hydrolases; C513132:PrtV protein, Vibrio cholerae
keywords: N-terminal domain; NMR; PrtV; Vibrio cholera; metalloproteases