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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia)

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Autor(es):
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Watanabe, Leandra [1] ; de Moura, Patricia Ribeiro [1] ; Bleicher, Lucas [1] ; Nascimento, Alessandro S. [1] ; Zamorano, Laura S. [2] ; Calvete, Juan J. [3] ; Sanz, Libia [3] ; Perez, Alicia [3] ; Bursakov, Sergey [4] ; Roig, Manuel G. [2] ; Shnyrov, Valery L. [5] ; Polikarpov, Igor [1]
Número total de Autores: 12
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Dept Fis & Informat, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Salamanca, Dept Quim Fis, Fac Quim, E-37008 Salamanca - Spain
[3] CSIC, Inst Biomed Valencia, Valencia 46010 - Spain
[4] Univ Nova Lisboa, REQUIMTE, Dept Quim, Ctr Quim Fina & Biotecnol, Fac Ciencias & Tecnol, P-2829516 Caparica - Portugal
[5] Univ Salamanca, Fac Biol, Dept Bioquim & Biol Mol, Salamanca 37007 - Spain
Número total de Afiliações: 5
Tipo de documento: Artigo Científico
Fonte: Journal of Structural Biology; v. 169, n. 2, p. 226-242, Feb. 2010.
Área do conhecimento: Ciências Biológicas - Biofísica
Notas: O processo está em nome de Igor Polikarpov que faz parte da autoria do artigo
Citações Web of Science: 33
Assunto(s):Biofísica   Cristalografia física   Enzimas   Peroxidase   Plantas extrativas   Palmeiras   Roystonea regia
Resumo

Royal palm tree peroxidase (RPTP) is a very stable enzyme in regards to acidity, temperature, H2O2, and organic solvents. Thus, RPTP is a promising candidate for developing H2O2-sensitive biosensors for diverse applications in industry and analytical chemistry. RPTP belongs to the family of class III secretory plant peroxidases, which include horseradish peroxidase isozyme C, soybean and peanut peroxidases. Here we report the X-ray structure of native RPTP isolated from royal palm tree (Roystonea regia) refined to a resolution of 1.85 Å. RPTP has the same overall folding pattern of the plant peroxidase superfamily, and it contains one heme group and two calcium-binding sites in similar locations. The three-dimensional structure of RPTP was solved for a hydroperoxide complex state, and it revealed a bound 2-(N-morpholino) ethanesulfonic acid molecule (MES) positioned at a putative substrate-binding secondary site. Nine N-glycosylation sites are clearly defined in the RPTP electron-density maps, revealing for the first time conformations of the glycan chains of this highly glycosylated enzyme. Furthermore, statistical coupling analysis (SCA) of the plant peroxidase superfamily was performed. This sequence-based method identified a set of evolutionarily conserved sites that mapped to regions surrounding the heme prosthetic group. The SCA matrix also predicted a set of energetically coupled residues that are involved in the maintenance of the structural folding of plant peroxidases. The combination of crystallographic data and SCA analysis provides information about the key structural elements that could contribute to explaining the unique stability of RPTP. (AU)

Processo FAPESP: 06/00182-8 - Biofísica estrutural dos receptores nucleares e proteínas relacionadas
Beneficiário:Igor Polikarpov
Linha de fomento: Auxílio à Pesquisa - Temático