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Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae

Journal article
Authors A. Edwin
Cecilia Persson
Maxim Mayzel
S. N. Wai
A. Ohman
B Göran Karlsson
A. E. Sauer-Eriksson
Published in Protein Science
Volume 24
Issue 12
Pages 2076-2080
ISSN 0961-8368
Publication year 2015
Published at Swedish NMR Centre at Göteborg University
Pages 2076-2080
Language en
Links dx.doi.org/10.1002/pro.2815
Keywords Vibrio cholera, metalloproteases, PrtV, N-terminal domain, NMR, purification, expression, software, server, Biochemistry & Molecular Biology
Subject categories Biochemistry and Molecular Biology, Molecular biology

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 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.

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