Ontology highlight
ABSTRACT:
SUBMITTER: Edwin A
PROVIDER: S-EPMC4815223 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Edwin Aaron A Persson Cecilia C Mayzel Maxim M Wai Sun Nyunt SN Öhman Anders A Karlsson B Göran BG Sauer-Eriksson A Elisabeth AE
Protein science : a publication of the Protein Society 20151106 12
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) ...[more]