Cross-linking mass spectrometry reveals structural insights of the glutamine synthetase from Leishmania braziliensis

dc.creatorLima, Jhenifer Yonara de
dc.creatorSantos, Marlon Dias Mariano
dc.creatorMurakami, Mario Tyago
dc.creatorCarvalho, Paulo Costa
dc.creatorSouza, Tatiana de Arruda Campos Brasil de
dc.date2022-03-24T13:49:03Z
dc.date2022-03-24T13:49:03Z
dc.date2021
dc.date.accessioned2023-09-26T20:27:53Z
dc.date.available2023-09-26T20:27:53Z
dc.identifierLIMA, Jhenifer Yonara de et al. Cross-linking mass spectrometry reveals structural insights of the glutamine synthetase from Leishmania braziliensis. Mem. Inst. Oswaldo Cruz, V. 116, n. e210209, p. 1–7, 2021.
dc.identifier1678-8060
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/51852
dc.identifier10.1590/0074-02760210209
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8857496
dc.descriptionLeishmaniasis is a neglected tropical disease caused by the parasite Leishmania braziliensis, commonly found in Brazil and associated with cutaneous and visceral forms of this disease. Like other organisms, L. braziliensis has an enzyme called glutamine synthetase (LbGS) that acts on the synthesis of glutamine from glutamate. This enzyme plays an essential role in the metabolism of these parasites and can be a potential therapeutic target for treating this disease. This study Investigate LbGS structure and generate structural models of the protein. We use the method of crosslinking mass spectrometry (XLMS) and generate structural models in silico using I-TASSER. FINDINGS 42 XLs peptides were identified, of which 37 are explained in a monomeric model with the other five indicating LbGS dimerization and pentamers interaction region. The comparison of 3D models generated in the presence and absence of XLMS restrictions probed the benefits of modeling with XLMS highlighting the inappropriate folding due to the absence of spatial restrictions. In conclusion, we disclose the conservation of the active site and interface regions, but also unique features of LbGS showing the potential of XLMS to probe structural information and explore new drugs.
dc.formatapplication/pdf
dc.languagepor
dc.publisherFundação Oswaldo Cruz. Instituto Oswaldo Cruz
dc.rightsopen access
dc.subjectProteomics
dc.subjectProteins
dc.subjectGlutamate-Ammonia Ligase
dc.subjectLeishmania braziliensis
dc.subjectProteómica
dc.subjectProteínas
dc.subjectGlutamato-Amoníaco Ligasa
dc.subjectLeishmania braziliensis
dc.subjectProtéomique
dc.subjectProtéines
dc.subjectGlutamate-ammonia ligase
dc.subjectLeishmania brasiliensis
dc.subjectProteômica
dc.subjectProteínas
dc.subjectGlutamina Sintetase
dc.subjectLeishmania braziliensis
dc.titleCross-linking mass spectrometry reveals structural insights of the glutamine synthetase from Leishmania braziliensis
dc.typeArticle


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