Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae
2015 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 24, no 12, 2076-2080 p.Article in journal (Refereed) PublishedText
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 alpha-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.
Place, publisher, year, edition, pages
2015. Vol. 24, no 12, 2076-2080 p.
Vibrio cholera, metalloproteases, PrtV, N-terminal domain, NMR, LAGLIO F, 1995, JOURNAL OF BIOMOLECULAR NMR, V6, P277 inoda Sumio, 2011, BIOCONTROL SCIENCE, V16, P1 lm L., 2008, BIOINFORMATICS, V24, P2780 itkevicius Karolis, 2008, FEBS JOURNAL, V275, P3167 itkevicius K, 2006, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES
Microbiology in the medical area
IdentifiersURN: urn:nbn:se:umu:diva-116102DOI: 10.1002/pro.2815ISI: 000368292000017PubMedID: 26434928OAI: oai:DiVA.org:umu-116102DiVA: diva2:901527