ArticlePlanta2011
Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.
Article in Planta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
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- Protease-bound structure of Ricistatin provides insights into the mechanism of action of tick salivary cystatins in the vertebrate host.Cellular and molecular life sciences : CMLS · 2023Article
- AlphaFold-Multimer predicts cross-kingdom interactions at the plant-pathogen interface.Nature communications · 2023Article
- A novel cysteine proteinase inhibitor from seeds ofBiochemistry and biophysics reports · 2021Article
- Papain-like cysteine proteinase zone (PCP-zone) and PCP structural catalytic core (PCP-SCC) of enzymes with cysteine proteinase fold.International journal of biological macromolecules · 2020Article
- Article
- Article
- Phytocystatins: Defense Proteins against Phytophagous Insects and Acari.International journal of molecular sciences · 2016Review
- Rice bifunctional phytocystatin is a dual modulator of legumain and papain-like proteases.Plant molecular biology · 2016Article
- TcCYPR04, a Cacao Papain-Like Cysteine-Protease Detected in Senescent and Necrotic Tissues Interacts with a Cystatin TcCYS4.PloS one · 2015Article
- Functional characterization of the N-terminal and C-terminal domains of a sesame group II phytocystatin.Botanical studies · 2014Article
- The diversity of rice phytocystatins.Molecular genetics and genomics : MGG · 2014Article
- Cysteine protease and cystatin expression and activity during soybean nodule development and senescence.BMC plant biology · 2014Article
- Botany. Pathogen specialization.Science (New York, N.Y.) · 2014Article
- Atomic-accuracy prediction of protein loop structures through an RNA-inspired Ansatz.PloS one · 2013Article
- Solution structure of a phytocystatin from Ananas comosus and its molecular interaction with papain.PloS one · 2012Article
- A model of the C14-EPIC complex indicates hotspots for a protease-inhibitor arms race in the oomycete-potato interaction.Plant signaling & behavior · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tarocystatin (CeCPI) from taro (Colocasia esculenta cv. Kaohsiung no. 1), a group-2 phytocystatin, shares a conserved N-terminal cystatin domain (NtD) with other phytocystatins but contains a C-terminal cystatin-like extension (CtE). The structure of the tarocystatin-papain complex and the domain interaction between NtD and CtE in tarocystatin have not been determined. We resolved the crystal structure of the phytocystatin-papain complex at resolution 2.03 Å. Surprisingly, the structure of the NtD-papain complex in a stoichiometry of 1:1 could be built, with no CtE observed. Only two remnant residues of CtE could be built in the structure of the CtE-papain complex. Therefore, CtE is easily digested by papain. To further characterize the interaction between NtD and CtE, three segments of tarocystatin, including the full-length (FL), NtD and CtE, were used to analyze the domain-domain interaction and the inhibition ability. The results from glutaraldehyde cross-linking and yeast two-hybrid assay indicated the existence of an intrinsic flexibility in the region linking NtD and CtE for most tarocystatin molecules. In the inhibition activity assay, the glutathione-S-transferase (GST)-fused FL showed the highest inhibition ability without residual peptidase activity, and GST-NtD and FL showed almost the same inhibition ability, which was higher than with NtD alone. On the basis of the structures, the linker flexibility and inhibition activity of tarocystatins, we propose that the overhangs from the cystatin domain may enhance the inhibition ability of the cystatin domain against papain.
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