ArticleThe Plant cell2009
Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins.
Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 59 citations in OpenAlex.
- Importance of Secondary Structure Data in Large Scale Protein Modeling Using Low-Resolution SURPASS Method.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Gradual Analytics of Starch-Interacting Proteins Revealed the Involvement of Starch-Phosphorylating Enzymes during Synthesis of Storage Starch in Potato (Molecules (Basel, Switzerland) · 2023Article
- Ab initio phasing of the diffraction of crystals with translational disorder.Acta crystallographica. Section A, Foundations and advances · 2019Article
- Recombinant protein susceptibility to proteolysis in the plant cell secretory pathway is pH-dependent.Plant biotechnology journal · 2018Article
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- Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway.Scientific reports · 2015Article
- Functional characterization of the N-terminal and C-terminal domains of a sesame group II phytocystatin.Botanical studies · 2014Article
- Characterization of Solanum tuberosum multicystatin and the significance of core domains.The Plant cell · 2013Article
- Solution structure of a phytocystatin from Ananas comosus and its molecular interaction with papain.PloS one · 2012Article
- Post-translational regulation and trafficking of the granulin-containing protease RD21 of Arabidopsis thaliana.PloS one · 2012Article
- Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins.Planta · 2011Article
- A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants.Transgenic research · 2011Article
- Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases.Plant cell reports · 2011Article
- Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination.Plant physiology · 2009Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Potato (Solanum tuberosum) multicystatin (PMC) is a crystalline Cys protease inhibitor present in the subphellogen layer of potato tubers. It consists of eight tandem domains of similar size and sequence. Our in vitro results showed that the pH/PO(4)(-)-dependent oligomeric behavior of PMC was due to its multidomain nature and was not a characteristic of the individual domains. Using a single domain of PMC, which still maintains inhibitor activity, we identified a target protein of PMC, a putative Cys protease. In addition, our crystal structure of a representative repeating unit of PMC, PMC-2, showed structural similarity to both type I and type II cystatins. The N-terminal trunk, alpha-helix, and L2 region of PMC-2 were most similar to those of type I cystatins, while the conformation of L1 more closely resembled that of type II cystatins. The structure of PMC-2 was most similar to the intensely sweet protein monellin from Dioscorephyllum cumminisii (serendipity berry), despite a low level of sequence similarity. We present a model for the possible molecular organization of the eight inhibitory domains in crystalline PMC. The unique molecular properties of the oligomeric PMC crystal are discussed in relation to its potential function in regulating the activity of proteases in potato tubers.
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