1H, 15N and 13C backbone assignments and secondary structures of c-ter100 domain of vibrio extracellular metalloprotease derived from vibrio vulnificus

Ji Hye Yun, Heeyoun Kim, Jung Eun Park, Hae Kap Cheong, Chaejoon Cheong, Jung Sup Lee, Weontae Lee

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Vibrio extracellular metalloprotease (vEP), secreted from Vibrio vulnificus, shows various proteolytic function such as prothrombin activation and fibrinolytic activities. Premature form of vEP has an N-terminal (nPP) and a C-terminal (C-ter100) region. The nPP and C-ter100 regions are autocleaved for the matured metalloprotease activity. It has been proposed that two regions play a key role in regulating enzymatic activity of vEP. Especially, C-ter100 has a regulatory function on proteolytic activity of vEP. C-ter100 domain has been cloned into the E. coli expression vectors, pET 32a and pGEX 4T-1 with TEV protease cleavage site and purified using gel-filtration chromatography followed by affinity chromatography. To understand how C-ter100 modulates proteolytic activity of vEP, structural studies were performed by heteronuclar multi-dimensional NMR spectroscopy. Backbone 1H, 15N and 13C resonances were assigned by data from standard triple resonance and HCCH-TOCSY experiments. The secondary structures of vEP C-ter100 were determined by TALOS+ and CSI software based on hydrogen/deuterium exchange. NMR data show that C-ter100 of vEP forms a β-barrel structure consisting of eight β-strands.

Original languageEnglish
Pages (from-to)3248-3252
Number of pages5
JournalBulletin of the Korean Chemical Society
Issue number10
Publication statusPublished - 2012 Oct 20


All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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