Resonance assignments and secondary structure of a phytocystatin from Sesamum indicum

Yu Jun Hu, Deli Irene, Chi Jen Lo, Yong Liang Cai, T. C. Tzen, Ta Hsien Lin, Chia Lin Chyan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

A cDNA encoding a cysteine protease inhibitor, cystatin was cloned from sesame (Sesamum indicum L.) seed. This clone was constructed into an expression vector and expressed in E. coli and purified to homogeneous. The recombinant sesame cystatin (SiCYS) showed effectively inhibitory activity toward C1 cysteine proteases. In order to unravel its inhibitory action from structural point of view, multidimensional heteronuclear NMR techniques were used to characterize the structure of SiCYS. The full 1H, 15N, and 13C resonances of SiCYS were assigned. The secondary structure of SiCYS was identified by using the assigned chemical shifts of 1Hα, 13Cα, 13Cβ, and 13CO through the consensus chemical shift index (CSI). The results of CSI analysis of SiCYS suggest eight β-strands (residues 33–46, 51–61, 63–75, 80–87, 150–155, 157–169, 172–183, and 192–195) and two α-helices (residues 16–30, and 120–135).

Original languageEnglish
Pages (from-to)309-311
Number of pages3
JournalBiomolecular NMR Assignments
Volume9
Issue number2
DOIs
StatePublished - 22 Oct 2015

Keywords

  • Cystatin
  • Cysteine protease inhibitor
  • Phytocystatin
  • Protein NMR

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