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User:Plinio Vieira
Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of Mario Murakami. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at Brazilian National Center for Research in Energy and Materials under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from Xanthomonas that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of Miguel Alcalde at Institute of Catalysis and Petrochemistry, focusing on the random and semi-rational evolution of a GH35 β-galactosidase. He currently works as Researcher Specialist at Brazilian Biorenewables Laboratory, focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:
- CE20 Family first Xanthomonas citri pv. citri xyloglucan acetylesterase PDB ID 7KMM [1]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase PDB ID 6BYC [2]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase, in complex with mannose PDB ID 6BYE [2]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase mutant E477A PDB ID 6BYI [1]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase mutant E575A PDB ID 6BYG [2]
- GH31 Xanthomonas citri pv. citri exo-α-xylosidase PDB ID 7KMP [3]
- GH31 Xanthomonas citri pv. citri exo-α-xylosidase, in complex with xylose PDB ID 7KNC [4]
- GH35 Xanthomonas citri pv. citri exo-β-galactosidase PDB ID 7KMN [5]
- GH35 Xanthomonas citri pv. citri exo-β-galactosidase, in complex with galactose PDB ID 7KMO [6]
- GH74 Xanthomonas campestris pv. campestris endo-xyloglucanase, in complex with XG oligosaccharide PDB ID 7KN8 [7]
- GH95 Xanthomonas citri pv. citri α-L-1,2-fucosidase PDB ID 7KMQ [8]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose PDB ID 6UAU [9]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E102A mutant, in complex with laminaripentaose PDB ID 6UAT [10]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199Q mutant PDB ID 6UBFZ [11]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199A mutant, in complex with laminaripentaose PDB ID 6UAS [12]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199A mutant, in complex with laminarihexaose PDB ID 6UFL [13]
- GH128 Sorangium cellulosum endo-β-1,3-glucanase PDB ID 6UAX [14]
- GH128 Lentinula edodes endo-β-1,3-glucanase PDB ID 6UB2 [15]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase PDB ID 6UB8 [16]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase, in complex with laminaritriose PDB ID 6UAB [17]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase, with laminaribiose at the surface-binding site PDB ID 6UBB [18]
- GH128 Cryptococcus neoformans oligosaccharide-binding protein PDB ID 6UBC [19]
- Vieira PS, Bonfim IM, Araujo EA, Melo RR, Lima AR, Fessel MR, Paixão DAA, Persinoti GF, Rocco SA, Lima TB, Pirolla RAS, Morais MAB, Correa JBL, Zanphorlin LM, Diogo JA, Lima EA, Grandis A, Buckeridge MS, Gozzo FC, Benedetti CE, Polikarpov I, Giuseppe PO, and Murakami MT. (2021). Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors. Nat Commun. 2021;12(1):4049. DOI:10.1038/s41467-021-24277-4 |
- Domingues MN, Souza FHM, Vieira PS, de Morais MAB, Zanphorlin LM, Dos Santos CR, Pirolla RAS, Honorato RV, de Oliveira PSL, Gozzo FC, and Murakami MT. (2018). Structural basis of exo-β-mannanase activity in the GH2 family. J Biol Chem. 2018;293(35):13636-13649. DOI:10.1074/jbc.RA118.002374 |
- Santos CR, Costa PACR, Vieira PS, Gonzalez SET, Correa TLR, Lima EA, Mandelli F, Pirolla RAS, Domingues MN, Cabral L, Martins MP, Cordeiro RL, Junior AT, Souza BP, Prates ÉT, Gozzo FC, Persinoti GF, Skaf MS, and Murakami MT. (2020). Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family. Nat Chem Biol. 2020;16(8):920-929. DOI:10.1038/s41589-020-0554-5 |