Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia)
| Autor: | Valery L. Shnyrov, Manuel G. Roig, Libia Sanz, Alicia Pérez, Igor Polikarpov, Juan J. Calvete, Patricia Ribeiro de Moura, Laura S. Zamorano, Lucas Bleicher, Leandra Watanabe, Sergey A. Bursakov, Alessandro S. Nascimento |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular animal structures DNA Complementary Glycosylation Sequence analysis Stereochemistry Protein Conformation Molecular Sequence Data Horseradish peroxidase chemistry.chemical_compound Protein structure Structural Biology Tandem Mass Spectrometry Araceae Amino Acid Sequence BIOLOGIA MOLECULAR VEGETAL Heme Peptide sequence DNA Primers Peroxidase biology Base Sequence Chemistry Sequence Analysis DNA Kinetics Biochemistry embryonic structures biology.protein Statistical coupling analysis Ethanesulfonic acid Crystallization |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 1095-8657 |
| Popis: | Royal palm tree peroxidase (RPTP) is a very stable enzyme in regards to acidity, temperature, H(2)O(2), and organic solvents. Thus, RPTP is a promising candidate for developing H(2)O(2)-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 1.85A. 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. |
| Databáze: | OpenAIRE |
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