%0 Journal Article %1 WOS:000557874400033 %A Cruz, Wallace T %A Bezerra, Eduardo H S %A V, Marcio Ramos %A Rocha, Bruno A M %A Medina, Maria C %A Demarco, Diego %A Carvalho, Cristina Paiva S %A Oliveira, Jefferson S %A Sousa, Jeanlex S %A Souza, Pedro F N %A Freire, Valder N %A da Silva, Francisca M S %A Freitas, Cleverson D T %C ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000, IRELAND %D 2020 %I ELSEVIER IRELAND LTD %J PLANT SCIENCE %K Articulated Cysteine Latex} laticifer; protease; {Apocynaceae; %R 10.1016/j.plantsci.2020.110590 %T Crystal structure and specific location of a germin-like protein with proteolytic activity from Thevetia peruviana %V 298 %X Peruvianin-I is a cysteine peptidase (EC 3.4.22) purified from Thevetia peruviana. Previous studies have shown that it is the only germin-like protein (GLP) with proteolytic activity described so far. In this work, the X-ray crystal structure of peruvianin-I was determined to a resolution of 2.15 angstrom (PDB accession number: 6ORM) and its specific location was evaluated by different assays. Its overall structure shows an arrangement composed of a homohexamer (a trimer of dimers) where each monomer exhibits a typical beta-barrel fold and two glycosylation sites (Asn(55) and Asn(1)(44)). Analysis of its active site confirmed the absence of essential amino acids for typical oxalate oxidase activity of GLP5. Details of the active site and molecular docking results, using a specific cysteine peptidase inhibitor (iodoacetamide), were used to discuss a plausible mechanism for proteolytic activity of peruvianin-I. Histological analyses showed that T. peruviana has articulated anastomosing laticifers, i.e., rows of cells which merge to form continuous tubes throughout its green organs. Moreover, peruvianin-I was detected exclusively in the latex. Because latex peptidases have been described as defensive molecules against insects, we hypothesize that peruvianin-I contributes to protect T. peruviana plants against herbivory.

@article{WOS:000557874400033, abstract = {Peruvianin-I is a cysteine peptidase (EC 3.4.22) purified from Thevetia peruviana. Previous studies have shown that it is the only germin-like protein (GLP) with proteolytic activity described so far. In this work, the X-ray crystal structure of peruvianin-I was determined to a resolution of 2.15 angstrom (PDB accession number: 6ORM) and its specific location was evaluated by different assays. Its overall structure shows an arrangement composed of a homohexamer (a trimer of dimers) where each monomer exhibits a typical beta-barrel fold and two glycosylation sites (Asn(55) and Asn(1)(44)). Analysis of its active site confirmed the absence of essential amino acids for typical oxalate oxidase activity of GLP5. Details of the active site and molecular docking results, using a specific cysteine peptidase inhibitor (iodoacetamide), were used to discuss a plausible mechanism for proteolytic activity of peruvianin-I. Histological analyses showed that T. peruviana has articulated anastomosing laticifers, i.e., rows of cells which merge to form continuous tubes throughout its green organs. Moreover, peruvianin-I was detected exclusively in the latex. Because latex peptidases have been described as defensive molecules against insects, we hypothesize that peruvianin-I contributes to protect T. peruviana plants against herbivory.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000, IRELAND}, author = {Cruz, Wallace T and Bezerra, Eduardo H S and V, Marcio Ramos and Rocha, Bruno A M and Medina, Maria C and Demarco, Diego and Carvalho, Cristina Paiva S and Oliveira, Jefferson S and Sousa, Jeanlex S and Souza, Pedro F N and Freire, Valder N and da Silva, Francisca M S and Freitas, Cleverson D T}, biburl = {https://www.bibsonomy.org/bibtex/25e680b6420de45ae8c75397c27e0fa6c/ppgfis_ufc_br}, doi = {10.1016/j.plantsci.2020.110590}, interhash = {aa9478265f08531380871e89a8d63c7d}, intrahash = {5e680b6420de45ae8c75397c27e0fa6c}, issn = {0168-9452}, journal = {PLANT SCIENCE}, keywords = {Articulated Cysteine Latex} laticifer; protease; {Apocynaceae;}, publisher = {ELSEVIER IRELAND LTD}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Crystal structure and specific location of a germin-like protein with proteolytic activity from Thevetia peruviana}, tppubtype = {article}, volume = 298, year = 2020 }